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Articles de revues sur le sujet « Charged-residue »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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1

Armstrong, K. M., and R. L. Baldwin. "Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges." Proceedings of the National Academy of Sciences 90, no. 23 (1993): 11337–40. http://dx.doi.org/10.1073/pnas.90.23.11337.

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To determine whether a charged histidine side chain affects alpha-helix stability only when histidine is close to one end of the helix or also when it is in the central region, we substitute a single histidine residue at many positions in two reference peptides and measure helix stability and histidine pKa. The position of a charged histidine residue has a major effect on helix stability in 0.01 M NaCl: the helix content of a 17-residue peptide is 24% when histidine is at position 3 compared to 76% when it is at position 17. This dependence of helix content on histidine position decreases shar

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Zhang, Zhao, Yanfang Xu, Pei Hong Dong, Dipika Sharma, and Nipavan Chiamvimonvat. "A negatively charged residue in the outer mouth of rat sodium channel determines the gating kinetics of the channel." American Journal of Physiology-Cell Physiology 284, no. 5 (2003): C1247—C1254. http://dx.doi.org/10.1152/ajpcell.00471.2002.

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Previous studies using combined techniques of site-directed mutagenesis and electrophysiology of voltage-gated Na+ channels have demonstrated that there are significant overlaps in the regions that are important for the two fundamental properties of the channels, namely gating and permeation. We have previously shown that a pore-lining residue, W402 in S5-S6 region (P loop) in domain I of the μ1 skeletal muscle Na+channel, was important in the gating of the channel. Here, we determined the role of an adjacent pore-lining negatively charged residue (E403) in channel gating. Charge neutralizatio

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Lemire, Isabelle, Patrice Roy, and Guy Boileau. "Translocation of neutral endopeptidase 24.11 mutants with deletions of the NH2- terminal cytosolic domain." Biochemistry and Cell Biology 72, no. 5-6 (1994): 182–87. http://dx.doi.org/10.1139/o94-027.

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Rabbit neutral endopeptidase 24.11 (NEP) is a type II membrane protein with a positively charged 27 amino acid residue NH2-terminal cytoplasmic domain, a 20 amino acid residue hydrophobic signal peptide/membrane anchor domain, and a large catalytic COOH-terminal domain exposed on the exoplasmic side of the membrane. To study the role of the cytosolic domain in anchoring NEP in the plasma membrane, we constructed two mutants in which this cytosolic domain was deleted. In the first mutant (NEPΔcyto), a Glu residue was present in NH2-terminus, while a Lys residue was substituted at the same posit

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Kalchenko, Vitaly, Olga Kalchenko, and Sergiy Cherenok. "Complexation of Calix[4]arene bis-Hydroxymethylenediphosphonic Acid with Amino acids. Binding Constants Determination by RP HPLC Method." French-Ukrainian Journal of Chemistry 3, no. 2 (2015): 93–100. http://dx.doi.org/10.17721/fujcv3i2p93-100.

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Host-Guest complexation of calixarene-bis-hydroxymethylenediphosphonic acid with 17 amino acids in water solution had been studied by the RP HPLC and molecular modelling methods. It had been shown the binding constants of the complexes are depended on the nature of the amino acid residue, log P and pKa of the acids. The complexation is mainly determined by the electrostatic interactions between the positively charged nitrogen atom of the amino acid and the negatively charged oxygen atom of phosphonic acid residue of the calixarene, the Host-Guest p-p, СН-p and solvophobic interactions.

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Fernandez de la Mora, J. "Electrospray ionization of large multiply charged species proceeds via Dole’s charged residue mechanism." Analytica Chimica Acta 406, no. 1 (2000): 93–104. http://dx.doi.org/10.1016/s0003-2670(99)00601-7.

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Mayol, Eduardo, Mercedes Campillo, Arnau Cordomí, and Mireia Olivella. "Inter-residue interactions in alpha-helical transmembrane proteins." Bioinformatics 35, no. 15 (2018): 2578–84. http://dx.doi.org/10.1093/bioinformatics/bty978.

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Abstract Motivation The number of available membrane protein structures has markedly increased in the last years and, in parallel, the reliability of the methods to detect transmembrane (TM) segments. In the present report, we characterized inter-residue interactions in α-helical membrane proteins using a dataset of 3462 TM helices from 430 proteins. This is by far the largest analysis published to date. Results Our analysis of residue–residue interactions in TM segments of membrane proteins shows that almost all interactions involve aliphatic residues and Phe. There is lack of polar–polar, po

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Mahdavi, Atiyeh, Reza H. Sajedi, Saman Hosseinkhani, and Majid Taghdir. "Hyperactive Arg39Lys mutated mnemiopsin: implication of positively charged residue in chromophore binding cavity." Photochemical & Photobiological Sciences 14, no. 4 (2015): 792–800. http://dx.doi.org/10.1039/c4pp00191e.

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Mnemiopsin, a Ca<sup>2+</sup>-regulated photoprotein isolated fromMnemiopsis leidyi, belongs to the family of ctenophore photoproteins. While there are no charged amino acid residues in the coelenterazine binding cavity of cnidarian photoproteins, ctenophore photoproteins have a positively charged residue (Arg) in this region.

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Miniero, Daniela Valeria, Magnus Monné, Maria Antonietta Di Noia, Luigi Palmieri, and Ferdinando Palmieri. "Evidence for Non-Essential Salt Bridges in the M-Gates of Mitochondrial Carrier Proteins." International Journal of Molecular Sciences 23, no. 9 (2022): 5060. http://dx.doi.org/10.3390/ijms23095060.

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Mitochondrial carriers, which transport metabolites, nucleotides, and cofactors across the mitochondrial inner membrane, have six transmembrane α-helices enclosing a translocation pore with a central substrate binding site whose access is controlled by a cytoplasmic and a matrix gate (M-gate). The salt bridges formed by the three PX[DE]XX[RK] motifs located on the odd-numbered transmembrane α-helices greatly contribute to closing the M-gate. We have measured the transport rates of cysteine mutants of the charged residue positions in the PX[DE]XX[RK] motifs of the bovine oxoglutarate carrier, t

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He, Yuxian, Shuwen Liu, Jingjing Li, et al. "Conserved Salt Bridge between the N- and C-Terminal Heptad Repeat Regions of the Human Immunodeficiency Virus Type 1 gp41 Core Structure Is Critical for Virus Entry and Inhibition." Journal of Virology 82, no. 22 (2008): 11129–39. http://dx.doi.org/10.1128/jvi.01060-08.

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ABSTRACT The fusogenic human immunodeficiency virus type 1 (HIV-1) gp41 core structure is a stable six-helix bundle formed by its N- and C-terminal heptad repeat sequences. Notably, the negatively charged residue Asp632 located at the pocket-binding motif in the C-terminal heptad repeat interacts with the positively charged residue Lys574 in the pocket formation region of the N-terminal heptad repeat to form a salt bridge. We previously demonstrated that the residue Lys574 plays an essential role in six-helix bundle formation and virus infectivity and is a key determinant of the target for ant

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Li, Yuan, Xing Li, Matthew Stremlau, Mark Lee та Joseph Sodroski. "Removal of Arginine 332 Allows Human TRIM5α To Bind Human Immunodeficiency Virus Capsids and To Restrict Infection". Journal of Virology 80, № 14 (2006): 6738–44. http://dx.doi.org/10.1128/jvi.00270-06.

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ABSTRACT Human TRIM5α (TRIM5αhu) only modestly inhibits human immunodeficiency virus type 1 (HIV-1) and does not inhibit simian immunodeficiency virus (SIVmac). Alteration of arginine 332 in the TRIM5αhu B30.2 domain to proline, the residue found in rhesus monkey TRIM5α, has been shown to create a potent restricting factor for both HIV-1 and SIVmac. Here we demonstrate that the potentiation of HIV-1 inhibition results from the removal of a positively charged residue at position 332 of TRIM5αhu. The increase in restricting activity correlated with an increase in the ability of TRIM5αhu mutants

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Schuldiner, Shimon, Dorit Granot, Sonia Steiner Mordoch, et al. "Small is Mighty: EmrE, a Multidrug Transporter as an Experimental Paradigm." Physiology 16, no. 3 (2001): 130–34. http://dx.doi.org/10.1152/physiologyonline.2001.16.3.130.

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EmrE is a multidrug transporter from Escherichia coli that functions as a homooligomer and is unique in its small size. In each monomer there are four tightly packed transmembrane segments and one membrane-embedded charged residue. This residue provides the basis for the coupling mechanism as part of a binding site “time shared” by substrates and protons.

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Ou, Xinwen, Bin Xue, Yichong Lao, et al. "Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability." Science Advances 6, no. 39 (2020): eabb7620. http://dx.doi.org/10.1126/sciadv.abb7620.

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Mussels can strongly adhere to hydrophilic minerals in sea habitats by secreting adhesive proteins. The adhesion ability of these proteins is often attributed to the presence of Dopa derived from posttranslational modification of Tyr, whereas the contribution of structural feature is overlooked. It remains largely unknown how adhesive proteins overcome the surface-bound water layer to establish underwater adhesion. Here, we use molecular dynamics simulations to probe the conformations of adhesive protein Pvfp-5β and its salt-tolerant underwater adhesion on superhydrophilic mica. Dopa and posit

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Verma, Sandhya, Valerie Bednar, Andrew Blount, and Brenda G. Hogue. "Identification of Functionally Important Negatively Charged Residues in the Carboxy End of Mouse Hepatitis Coronavirus A59 Nucleocapsid Protein." Journal of Virology 80, no. 9 (2006): 4344–55. http://dx.doi.org/10.1128/jvi.80.9.4344-4355.2006.

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ABSTRACT The coronavirus nucleocapsid (N) protein is a multifunctional viral gene product that encapsidates the RNA genome and also plays some as yet not fully defined role in viral RNA replication and/or transcription. A number of conserved negatively charged amino acids are located within domain III in the carboxy end of all coronavirus N proteins. Previous studies suggested that the negatively charged residues are involved in virus assembly by mediating interaction between the membrane (M) protein carboxy tail and nucleocapsids. To determine the importance of these negatively charged residu

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Shin, Youn-Chul, Sunju Park, and Wang-Shick Ryu. "A conserved arginine residue in the terminal protein domain of hepatitis B virus polymerase is critical for RNA pre-genome encapsidation." Journal of General Virology 92, no. 8 (2011): 1809–16. http://dx.doi.org/10.1099/vir.0.031914-0.

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Hepadnaviruses, including human hepatitis B virus (HBV) and duck hepatitis B virus (DHBV), replicate their DNA genome through reverse transcription. Although hepadnaviral polymerase (Pol) is distantly related to retroviral reverse transcriptases, some of its features are distinct. In particular, in addition to the reverse transcriptase and RNase H domains, which are commonly encoded by retroviral reverse transcriptases, the N-terminally extended terminal protein (TP) domain confers unique features such as protein-priming capability. Importantly, the TP domain is also essential for encapsidatio

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Moon, Hee-Jung, Manish Kumar Tiwari, Ranjitha Singh, Yun Chan Kang, and Jung-Kul Lee. "Molecular Determinants of the Cofactor Specificity of Ribitol Dehydrogenase, a Short-Chain Dehydrogenase/Reductase." Applied and Environmental Microbiology 78, no. 9 (2012): 3079–86. http://dx.doi.org/10.1128/aem.07751-11.

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ABSTRACTRibitol dehydrogenase fromZymomonas mobilis(ZmRDH) catalyzes the conversion of ribitol tod-ribulose and concomitantly reduces NAD(P)+to NAD(P)H. A systematic approach involving an initial sequence alignment-based residue screening, followed by a homology model-based screening and site-directed mutagenesis of the screened residues, was used to study the molecular determinants of the cofactor specificity of ZmRDH. A homologous conserved amino acid, Ser156, in the substrate-binding pocket of the wild-type ZmRDH was identified as an important residue affecting the cofactor specificity of Z

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Vostrikov, Vitaly V., Anna E. Daily, Denise V. Greathouse, and Roger E. Koeppe. "Charged or Aromatic Anchor Residue Dependence of Transmembrane Peptide Tilt." Journal of Biological Chemistry 285, no. 41 (2010): 31723–30. http://dx.doi.org/10.1074/jbc.m110.152470.

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Hogan, Christopher J., James A. Carroll, Henry W. Rohrs, Pratim Biswas, and Michael L. Gross. "Combined Charged Residue-Field Emission Model of Macromolecular Electrospray Ionization." Analytical Chemistry 81, no. 1 (2009): 369–77. http://dx.doi.org/10.1021/ac8016532.

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18

Eduljee, Cyrus, Thomas W. Claydon, Vijay Viswanathan, David Fedida, and Steven J. Kehl. "SCAM analysis reveals a discrete region of the pore turret that modulates slow inactivation in Kv1.5." American Journal of Physiology-Cell Physiology 292, no. 3 (2007): C1041—C1052. http://dx.doi.org/10.1152/ajpcell.00274.2006.

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In Kv1.5, protonation of histidine 463 in the S5-P linker (turret) increases the rate of depolarization-induced inactivation and decreases the peak current amplitude. In this study, we examined how amino acid substitutions that altered the physico-chemical properties of the side chain at position 463 affected slow inactivation and then used the substituted cysteine accessibility method (SCAM) to probe the turret region (E456-P468) to determine whether residue 463 was unique in its ability to modulate the macroscopic current. Substitutions at position 463 of small, neutral (H463G and H463A) or

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Chen, Mei-Fang, and Tsung-Yu Chen. "Side-chain Charge Effects and Conductance Determinants in the Pore of ClC-0 Chloride Channels." Journal of General Physiology 122, no. 2 (2003): 133–45. http://dx.doi.org/10.1085/jgp.200308844.

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The charge on the side chain of the internal pore residue lysine 519 (K519) of the Torpedo ClC-0 chloride (Cl−) channel affects channel conductance. Experiments that replace wild-type (WT) lysine with neutral or negatively charged residues or that modify the K519C mutant with various methane thiosulfonate (MTS) reagents show that the conductance of the channel decreases when the charge at position 519 is made more negative. This charge effect on the channel conductance diminishes in the presence of a high intracellular Cl− concentration ([Cl−]i). However, the application of high concentrations

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Bäckström, B. Thomas, Barbara T. Hausmann та Ed Palmer. "Signaling Efficiency of the T Cell Receptor Controlled by a Single Amino Acid in the β Chain Constant Region". Journal of Experimental Medicine 186, № 11 (1997): 1933–38. http://dx.doi.org/10.1084/jem.186.11.1933.

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A single amino acid residue, Gln136, located within the connecting peptide domain of Cβ controls the ability of the α/β TCR to transmit a full signal. TCRs in which this Cβ residue is mutated to Phe, the residue found in TCR-γ, are unresponsive to antigenic ligands. Interestingly, this Cβ residue is either polar or charged in every species studied thus far, including the trout and the skate. In contrast, the analogous residue in Cγ is always hydrophobic. In spite of their compromised antigen responsiveness, the mutant TCR complex contains the CD3-γ, -δ, -ε, and -ζ chains, and undergoes ζ chain

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Friedman, M. L., K. T. Schlueter, T. L. Kirley, and H. B. Halsall. "Fluorescence quenching of human orosomucoid. Accessibility to drugs and small quenching agents." Biochemical Journal 232, no. 3 (1985): 863–67. http://dx.doi.org/10.1042/bj2320863.

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The fluorescence behaviour of human orosomucoid was investigated. The intrinsic fluorescence was more accessible to acrylamide than to the slightly larger succinimide, indicating limited accessibility to part of the tryptophan population. Although I- showed almost no quenching, that of Cs+ was enhanced, and suggested a region of negative charge proximal to an emitting tryptophan residue. Removal of more than 90% of sialic acid from the glycan chains led to no change in the Cs+, I-, succinimide or acrylamide quenching, indicating that the negatively charged region originates with the protein co

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Yadav, Mohini, Manabu Igarashi, and Norifumi Yamamoto. "Theoretical insights into the molecular mechanism of I117V mutation in neuraminidase mediated reduction of oseltamivir drug susceptibility in A/H5N1 influenza virus." PeerJ Physical Chemistry 3 (November 22, 2021): e19. http://dx.doi.org/10.7717/peerj-pchem.19.

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The substitution of Ile to Val at residue 117 (I117V) of neuraminidase (NA) reduces the susceptibility of the A/H5N1 influenza virus to oseltamivir (OTV). However, the molecular mechanism by which the I117V mutation affects the intermolecular interactions between NA and OTV has not been fully elucidated. In this study, we performed molecular dynamics (MD) simulations to analyze the characteristic conformational changes that contribute to the reduced binding affinity of NA to OTV after the I117V mutation. The results of MD simulations revealed that after the I117V mutation in NA, the changes in

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Bogati, Bikash, Selene F. H. Shore, Thomas D. Nipper, Oana Stoiculescu, and Elizabeth M. Fozo. "Charged Amino Acids Contribute to ZorO Toxicity." Toxins 15, no. 1 (2022): 32. http://dx.doi.org/10.3390/toxins15010032.

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Chromosomally encoded toxin-antitoxin systems have been increasingly identified and characterized across bacterial species over the past two decades. Overproduction of the toxin gene results in cell growth stasis or death for the producing cell, but co-expression of its antitoxin can repress the toxic effects. For the subcategory of type I toxin-antitoxin systems, many of the described toxin genes encode a small, hydrophobic protein with several charged residues distributed across the sequence of the toxic protein. Though these charged residues are hypothesized to be critical for the toxic eff

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Moreau, Adrien, Pascal Gosselin-Badaroudine, and Mohamed Chahine. "Molecular biology and biophysical properties of ion channel gating pores." Quarterly Reviews of Biophysics 47, no. 4 (2014): 364–88. http://dx.doi.org/10.1017/s0033583514000109.

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AbstractThe voltage sensitive domain (VSD) is a pivotal structure of voltage-gated ion channels (VGICs) and plays an essential role in the generation of electrochemical signals by neurons, striated muscle cells, and endocrine cells. The VSD is not unique to VGICs. Recent studies have shown that a VSD regulates a phosphatase. Similarly, Hv1, a voltage-sensitive protein that lacks an apparent pore domain, is a self-contained voltage sensor that operates as an H+ channel.VSDs are formed by four transmembrane helices (S1–S4). The S4 helix is positively charged due to the presence of arginine and l

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Görbitz, Carl Henrik, and Vitthal N. Yadav. "N-(L-2-Aminopentanoyl)-L-phenylalanine dihydrate, a hydrophobic dipeptide with a nonproteinogenic residue." Acta Crystallographica Section C Crystal Structure Communications 69, no. 9 (2013): 1067–69. http://dx.doi.org/10.1107/s0108270113021914.

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The title dipeptide, better known as L-norvalyl-L-phenylalanine {systematic name: (S)-2-[(S)-2-aminopentanamido]-3-phenylpropanoic acid dihydrate}, C14H20N2O3·2H2O, has a nonproteinogenic N-terminal residue. In the solid state, it takes on a molecular conformation typical for one of the three classes of nanoporous dipeptides, but like two related compounds with a hydrophobic N-terminal residue and a C-terminal L-phenylalanine, it fails to form channels or pores. Instead, the crystal structure is divided into distinct hydrophobic and hydrophilic layers, the latter encompassing cocrystallized wa

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Willms, J. Alexander, Rita Beel, Martin L. Schmidt, Christian Mundt, and Marianne Engeser. "A new charge-tagged proline-based organocatalyst for mechanistic studies using electrospray mass spectrometry." Beilstein Journal of Organic Chemistry 10 (August 28, 2014): 2027–37. http://dx.doi.org/10.3762/bjoc.10.211.

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A new 4-hydroxy-L-proline derivative with a charged 1-ethylpyridinium-4-phenoxy substituent has been synthesized with the aim of facilitating mechanistic studies of proline-catalyzed reactions by ESI mass spectrometry. The charged residue ensures a strongly enhanced ESI response compared to neutral unmodified proline. The connection by a rigid linker fixes the position of the charge tag far away from the catalytic center in order to avoid unwanted interactions. The use of a charged catalyst leads to significantly enhanced ESI signal abundances for every catalyst-derived species which are the o

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Gonzalez, Carlos, Santiago Rebolledo, Marta E. Perez, and H. Peter Larsson. "Molecular mechanism of voltage sensing in voltage-gated proton channels." Journal of General Physiology 141, no. 3 (2013): 275–85. http://dx.doi.org/10.1085/jgp.201210857.

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Voltage-gated proton (Hv) channels play an essential role in phagocytic cells by generating a hyperpolarizing proton current that electrically compensates for the depolarizing current generated by the NADPH oxidase during the respiratory burst, thereby ensuring a sustained production of reactive oxygen species by the NADPH oxidase in phagocytes to neutralize engulfed bacteria. Despite the importance of the voltage-dependent Hv current, it is at present unclear which residues in Hv channels are responsible for the voltage activation. Here we show that individual neutralizations of three charged

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BERGERON, Eric, Ajoy BASAK, Etienne DECROLY, and Nabil G. SEIDAH. "Processing of alpha4 integrin by the proprotein convertases: histidine at position P6 regulates cleavage." Biochemical Journal 373, no. 2 (2003): 475–84. http://dx.doi.org/10.1042/bj20021630.

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The proprotein convertases (PCs) participate in the limited proteolysis of integrin α4 subunit at the H592VISKR597 ↓ ST site (where underlined residues indicate positively charged amino acids important for PC-mediated cleavage and ↓ indicates the cleavage site), since this cleavage is inhibited by the serpin α1-PDX (α1-antitrypsin Portland). Co-expression of α4 with each convertase in LoVo (furin-deficient human colon carcinoma) cells revealed that furin and proprotein convertase 5A (PC5A) are the best pro-α4 convertases. In agreement, processing of endogenous pro-α4 in human lymphoblastoid CE

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Dong, R. P., N. Kamikawaji, N. Toida, Y. Fujita, A. Kimura, and T. Sasazuki. "Characterization of T cell epitopes restricted by HLA-DP9 in streptococcal M12 protein." Journal of Immunology 154, no. 9 (1995): 4536–45. http://dx.doi.org/10.4049/jimmunol.154.9.4536.

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Abstract Interaction of the HLA-DP9 (DPA1*0201/DPB1*0901) molecule and M protein of serotype 12 (SS95/12) streptococci, a main component of the streptococcal cell wall Ag, has been investigated to decipher peptide-binding capacity and T cell activation in the context of the HLA-DP molecule. Seven antigenic peptides (amino acids 19-25) restricted by the HLA-DP9 molecule were identified in M12 protein, using M12 protein- or peptide-specific T cell lines from naturally exposed individuals. The binding affinity of each peptide to the HLA-DP9 molecule was measured by fluorescence intensity of bioti

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Pan, Ying, Lei Song, and Yuan Hu. "Effect of Calcium Ion Crosslinked Alginate Based Coating on Flame Retardancy of Polyester-Cotton Fabric." Materials Science Forum 909 (November 2017): 145–50. http://dx.doi.org/10.4028/www.scientific.net/msf.909.145.

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Bio-based and phosphorus-free coating was fabricated by layer-by-layer assembly method to obtain the flame retardant polyester-cotton fabric. For the first time, the modified polyester-cotton fabrics were prepared by utilizing positively charged polyethylenimine and negatively charged alginate together with subsequent crosslinking of calcium ion. Scanning electron microscopy and energy-dispersive X-ray demonstrated that the calcium ion crosslinked coating was successfully constructed on the substrate. The flame retardancy was investigated by horizontal flame test. The fire resistance of SA/PEI

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Trujillo, Adriana S., Karen H. Hsu, Meera C. Viswanathan, Anthony Cammarato, and Sanford I. Bernstein. "The R369 Myosin Residue within Loop 4 Is Critical for Actin Binding and Muscle Function in Drosophila." International Journal of Molecular Sciences 23, no. 5 (2022): 2533. http://dx.doi.org/10.3390/ijms23052533.

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The myosin molecular motor interacts with actin filaments in an ATP-dependent manner to yield muscle contraction. Myosin heavy chain residue R369 is located within loop 4 at the actin-tropomyosin interface of myosin’s upper 50 kDa subdomain. To probe the importance of R369, we introduced a histidine mutation of that residue into Drosophila myosin and implemented an integrative approach to determine effects at the biochemical, cellular, and whole organism levels. Substituting the similarly charged but bulkier histidine residue reduces maximal actin binding in vitro without affecting myosin ATPa

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Aubin, Chantal N. St, and Paul Linsdell. "Positive Charges at the Intracellular Mouth of the Pore Regulate Anion Conduction in the CFTR Chloride Channel." Journal of General Physiology 128, no. 5 (2006): 535–45. http://dx.doi.org/10.1085/jgp.200609516.

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Many different ion channel pores are thought to have charged amino acid residues clustered around their entrances. The so-called surface charges contributed by these residues can play important roles in attracting oppositely charged ions from the bulk solution on one side of the membrane, increasing effective local counterion concentration and favoring rapid ion movement through the channel. Here we use site-directed mutagenesis to identify arginine residues contributing important surface charges in the intracellular mouth of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl− c

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Ngo, Son Tung. "Computational Investigations of the Transmembrane Italian-Mutant (E22K) 3A\(\beta_{11 - 40}\) in Aqueous Solution." Communications in Physics 28, no. 3 (2018): 265. http://dx.doi.org/10.15625/0868-3166/28/3/12773.

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The Amyloid beta (Aβ) oligomers are characterized as critical cytotoxic materials in Alzheimer’s disease (AD) pathogenesis. Structural details of transmembrane oligomers are inevitably necessary to design/search potential inhibitor due to treat AD. However, the experimental detections for structural modify of low-order Aβ oligomers are precluded due to the extremely dynamic fluctuation of the oligomers. In this project, the transmembrane Italian-mutant (E22K) 3Aβ11-40 (tmE22K 3Aβ11-40) was extensively investigated upon the temperature replica exchange molecular dynamics (REMD) simulations. The

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Gäde, G. "A unique charged tyrosine-containing member of the adipokinetic hormone/red-pigment-concentrating hormone peptide family isolated and sequenced from two beetle species." Biochemical Journal 275, no. 3 (1991): 671–77. http://dx.doi.org/10.1042/bj2750671.

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An identical neuropeptide was isolated from the corpora cardiaca of two beetle species, Melolontha melolontha and Geotrupes stercorosus. Its primary structure was determined by pulsed-liquid-phase sequencing employing Edman chemistry after enzymically deblocking the N-terminal pyroglutamate residue. The C-terminus was also blocked, as indicated by the lack of digestion when the peptide was incubated with carboxypeptidase A. The sequence of this peptide, which is designated Mem-CC, is pGlu-Leu-Asn-Tyr-Ser-Pro-Asp-Trp-NH2. It is a new member of the adipokinetic hormone/red-pigment-concentrating

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Lin, Chen-Sheng, Wei-Jing Li, Chih-Yi Liao, et al. "A Reverse Mutation E143K within the PrM Protein of Zika Virus Asian Lineage Natal RGN Strain Increases Infectivity and Cytopathicity." Viruses 14, no. 7 (2022): 1572. http://dx.doi.org/10.3390/v14071572.

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Zika virus (ZIKV) is a positive-sense single-stranded RNA virus in the Flaviviridae, which is classified into two different lineages Asian and African. The outbreak of ZIKV Asian lineage isolates in 2015–2016 is associated with the increase in cases with prenatal microcephaly and Guillain–Barré syndrome, and has sparked attention throughout the world. Genome sequence alignment and the analysis of Asian and African lineage isolates indicate that amino acid changes, particular in positively charged amino acid substitutions in the pr region of prM protein might involve a phenotypic change that li

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Parrish, Jonathan C., J. Guy Guillemette, and Carmichael JA Wallace. "A tale of two charges: Distinct roles for an acidic and a basic amino acid in the structure and function of cytochrome c." Biochemistry and Cell Biology 79, no. 1 (2001): 83–91. http://dx.doi.org/10.1139/o00-083.

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Cytochrome c is a small electron transport protein found in the intermembrane space of mitochondria. As it interacts with a number of different physiological partners in a specific fashion, its structure varies little over eukaryotic evolutionary history. Two highly conserved residues found within its sequence are those at positions 13 and 90 (numbering is based on the standard horse cytochrome c); with single exceptions, residue 13 is either Lys or Arg, and residue 90 is either Glu or Asp. There have been conflicting views on the roles to be ascribed to these residues, particularly residue 13

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Hall, A., H. Dalbøge, A. Grubb, and M. Abrahamson. "Importance of the evolutionarily conserved glycine residue in the N-terminal region of human cystatin C (Gly-11) for cysteine endopeptidase inhibition." Biochemical Journal 291, no. 1 (1993): 123–29. http://dx.doi.org/10.1042/bj2910123.

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Human cystatin C variants in which the evolutionarily conserved Gly-11 residue has been replaced by residues with positively charged (Arg), negatively charged (Glu), bulky hydrophobic (Trp), or small (Ser or Ala) side-chains have been produced by site-directed mutagenesis and expression in Escherichia coli. The five variants were isolated and structurally verified. Their inhibitory properties were compared with those of wild-type recombinant cystatin C by determination of the equilibrium constants for dissociation (Ki) of their complexes with the cysteine endopeptidases papain and human cathep

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Redhu, Archana Kumari, Nitesh Kumar Khandelwal, Atanu Banerjee, Alexis Moreno, Pierre Falson, and Rajendra Prasad. "pHluorin enables insights into the transport mechanism of antiporter Mdr1: R215 is critical for drug/H+ antiport." Biochemical Journal 473, no. 19 (2016): 3127–45. http://dx.doi.org/10.1042/bcj20160407.

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Multidrug resistance 1 (MDR1) is a member of the major facilitator superfamily that contributes to MDR of Candida albicans. This antiporter belongs to the drug/H+ antiporter 1 family, pairing the downhill gradient of protons to drug extrusion. Hence, drug efflux from cytosol to extracellular space and the parallel import of H+ towards cytosol are inextricably linked processes. For monitoring the drug/H+ antiporter activity of Mdr1p, we developed a new system, exploiting a GFP variant pHluorin, which changes its fluorescence properties with pH. This enabled us to measure the cytosolic pH correl

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Gan, Lingmin, Yulang Chi, Yunhui Peng, et al. "Designing Analogs of SAAP-148 with Enhanced Antimicrobial and Anti-LPS Activities." International Journal of Molecular Sciences 25, no. 21 (2024): 11776. http://dx.doi.org/10.3390/ijms252111776.

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SAAP-148, a derivative of LL-37, exhibits a well-defined amphipathic structure and enhanced antimicrobial activity; however, it also displays significant cytotoxicity towards human cells. In this study, we employed Lys-scan to produce a series of amphiphilic SAAP-148 analogs derived from the SAAP-148 sequence to investigate the impact of the distribution of positively charged residues on the biological viability of the antimicrobial peptides (AMPs). The physical properties and biological activity of the designed peptides were subsequently compared. The substitution of lysine resulted in an inc

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Seica, Ana Filipa Santos, Cristina V. Iancu, Benedikt Pfeilschifter, M. Gregor Madej, Jun-Yong Choe, and Petra Hellwig. "Asp22 drives the protonation state of the Staphylococcus epidermidis glucose/H+ symporter." Journal of Biological Chemistry 295, no. 45 (2020): 15253–61. http://dx.doi.org/10.1074/jbc.ra120.014069.

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The Staphylococcus epidermidis glucose/H+ symporter (GlcPSe) is a membrane transporter highly specific for glucose and a homolog of the human glucose transporters (GLUT, SLC2 family). Most GLUTs and their bacterial counterparts differ in the transport mechanism, adopting uniport and sugar/H+ symport, respectively. Unlike other bacterial GLUT homologs (for example, XylE), GlcPSe has a loose H+/sugar coupling. Asp22 is part of the proton-binding site of GlcPSe and crucial for the glucose/H+ co-transport mechanism. To determine how pH variations affect the proton site and the transporter, we perf

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Choo, Liza Nuriati Lim Kim, Osumanu Haruna Ahmed, Nik Muhamad Nik Majid, and Zakry Fitri Abd Aziz. "Pineapple Residue Ash Reduces Carbon Dioxide and Nitrous Oxide Emissions in Pineapple Cultivation on Tropical Peat Soils at Saratok, Malaysia." Sustainability 13, no. 3 (2021): 1014. http://dx.doi.org/10.3390/su13031014.

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Burning pineapple residues on peat soils before pineapple replanting raises concerns on hazards of peat fires. A study was conducted to determine whether ash produced from pineapple residues could be used to minimize carbon dioxide (CO2) and nitrous oxide (N2O) emissions in cultivated tropical peatlands. The effects of pineapple residue ash fertilization on CO2 and N2O emissions from a peat soil grown with pineapple were determined using closed chamber method with the following treatments: (i) 25, 50, 70, and 100% of the suggested rate of pineapple residue ash + NPK fertilizer, (ii) NPK fertil

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Waelbroeck, M., J. Perret, P. Vertongen, M. Van Craenenbroeck, and P. Robberecht. "Identification of secretin, vasoactive intestinal peptide and glucagon binding sites: from chimaeric receptors to point mutations." Biochemical Society Transactions 30, no. 4 (2002): 437–41. http://dx.doi.org/10.1042/bst0300437.

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We have identified two basic residues that are important for the recognition of secretin and vasoactive intestinal peptide (VIP) by their respective receptors. These two peptides containing an Asp residue at position 3 interacted with an arginine residue in transmembrane helix 2 (TM2) of the receptor, and the lysine residue in extracellular loop 1 (ECL1) stabilized the active receptor conformation induced by the ligand. The glucagon receptor possesses a Lys instead of an Arg in TM2, and an Ile instead of Lys in ECL1; it markedly prefers a Gln side chain in position 3 of the ligand. Our results

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Ortega, Gabriel, Miguel A. Aguilar, Bishal K. Gautam, and Kevin W. Plaxco. "The effect of charged residue substitutions on the thermodynamics of protein‐surface interactions." Protein Science 30, no. 12 (2021): 2408–17. http://dx.doi.org/10.1002/pro.4215.

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Wei, Huiling, Jie Tan, Bingjie Zhou, Xiaotong Guan, Qiaoxian Zhong, and Jiaqi Wang. "Charged Residue Implantation Improves the Affinity of a Cross-Reactive Dengue Virus Antibody." International Journal of Molecular Sciences 23, no. 8 (2022): 4197. http://dx.doi.org/10.3390/ijms23084197.

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Dengue virus (DENV) has four serotypes that complicate vaccine development. Envelope protein domain III (EDIII) of DENV is a promising target for therapeutic antibody development. One EDIII-specific antibody, dubbed 1A1D-2, cross-reacts with DENV 1, 2, and 3 but not 4. To improve the affinity of 1A1D-2, in this study, we analyzed the previously solved structure of 1A1D-2-DENV2 EDIII complex. Mutations were designed, including A54E and Y105R in the heavy chain, with charges complementary to the epitope. Molecular dynamics simulation was then used to validate the formation of predicted salt brid

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Duraivelan, Kheerthana, Sagarika Dash, and Dibyendu Samanta. "An evolutionarily conserved charged residue dictates the specificity of heterophilic interactions among nectins." Biochemical and Biophysical Research Communications 534 (January 2021): 504–10. http://dx.doi.org/10.1016/j.bbrc.2020.11.052.

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Wible, Barbara A., Maurizio Taglialatela, Eckhard Ficker, and Arthur M. Brown. "Gating of inwardly rectifying K+ channels localized to a single negatively charged residue." Nature 371, no. 6494 (1994): 246–49. http://dx.doi.org/10.1038/371246a0.

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Page, Dana A., and Edgar C. Young. "A Charged Residue in the HCN Channel C-Linker Stabilizes the Open State." Biophysical Journal 110, no. 3 (2016): 282a. http://dx.doi.org/10.1016/j.bpj.2015.11.1525.

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Wang, Yunhua, Wenhu Wang, Junxia Lu, et al. "Preparation and characterization of some surface negatively charged residue mutants of cytochrome b5." Chinese Science Bulletin 46, no. 7 (2001): 555–58. http://dx.doi.org/10.1007/bf02900407.

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Dementieva, Ekaterina I., Elena A. Fedorchuk, Lubov Yu Brovko, Alexander P. Savitskii, and Natalya N. Ugarova. "Fluorescent Properties of Firefly Luciferases and Their Complexes with Luciferin." Bioscience Reports 20, no. 1 (2000): 21–30. http://dx.doi.org/10.1023/a:1005579016387.

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Fluorescence of luciferases from Luciola mingrelica (single tryptophanresidue, Trp-419) and Photinus pyralis (two tryptophan residues, Trp-417,Trp-426) was studied. Analysis of quenching of tryptophan fluorescenceshowed that the tryptophan residue conserved in all luciferases is notaccessible for charged quenchers, which is explained by the presence ofpositively and negatively charged amino acid residues in the close vicinityto it. An effective energy transfer from tryptophan to luciferin wasobserved during quenching of tryptophan fluorescence of both luciferaseswith luciferin. From the data o

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Lee, Song F., and Lingqiu Gao. "Mutational analysis of the C-terminal anchoring domains ofStreptococcus mutansP1 antigen: Role of the LPXTGX motif in P1 association with the cell wall." Canadian Journal of Microbiology 46, no. 6 (2000): 584–92. http://dx.doi.org/10.1139/w00-023.

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The salivary agglutinin-interacting adhesin P1 of Streptococcus mutans is anchored to the cell wall via the carboxy (C) terminus, which contains a wall-associated domain, a conserved LPXTGX motif, a hydrophobic domain, and a charged tail. To further investigate the role of the C-terminal anchoring regions in cell wall sorting and anchoring, mutational analysis was performed on P1 in this study. Three truncated P1 mutants and seven site-directed mutants were generated by a polymerase chain reaction-based technique. The mutated P1 genes were returned to the P1-negative S. mutans SM3352 for expre

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