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Relevant bibliographies by topics / Metal ion binding

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Academic literature on the topic 'Metal ion binding'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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Journal articles on the topic "Metal ion binding"

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MOHAN, ABHILASH, SHARMILA ANISHETTY, and PENNATHUR GAUTAM. "GLOBAL METAL-ION BINDING PROTEIN FINGERPRINT: A METHOD TO IDENTIFY MOTIF-LESS METAL-ION BINDING PROTEINS." Journal of Bioinformatics and Computational Biology 08, no. 04 (August 2010): 717–26. http://dx.doi.org/10.1142/s0219720010004884.

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Metal-ion binding proteins play a vital role in biological processes. Identifying putative metal-ion binding proteins is through knowledge-based methods. These involve the identification of specific motifs that characterize a specific class of metal-ion binding protein. Metal-ion binding motifs have been identified for the common metal ions. A robust global fingerprint that is useful in identifying a metal-ion binding protein from a non-metal-ion binding protein has not been devised. Such a method will help in identifying novel metal-ion binding proteins and proteins that do not possess a canonical metal-ion binding motif. We have used a set of physico-chemical parameters of metal-ion binding proteins encoded by the genes CzcA, CzcB and CzcD as a training set to supervised classifiers and have been able to identify several other metal ion binding proteins leading us to believe that metal-ion binding proteins have a global fingerprint, which cannot be pinned down to a single feature of the protein sequence.

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DiTusa, Charles A., Keith A. McCall, Trine Christensen, Mrinal Mahapatro, Carol A. Fierke, and Eric J. Toone. "Thermodynamics of Metal Ion Binding. 2. Metal Ion Binding by Carbonic Anhydrase Variants†." Biochemistry 40, no. 18 (May 2001): 5345–51. http://dx.doi.org/10.1021/bi0017327.

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Elinder, Fredrik, and Peter Århem. "Metal ion effects on ion channel gating." Quarterly Reviews of Biophysics 36, no. 4 (November 2003): 373–427. http://dx.doi.org/10.1017/s0033583504003932.

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1. Introduction 3742. Metals in biology 3783. The targets: structure and function of ion channels 3804. General effects of metal ions on channels 3824.1 Three types of general effect 3824.2 The main regulators 3835. Effects on gating: mechanisms and models 3845.1 Screening surface charges (Mechanism A) 3875.1.1 The classical approach 3875.1.1.1 Applying the Grahame equation 3885.1.2 A one-site approach 3915.2 Binding and electrostatically modifying the voltage sensor (Mechanism B) 3915.2.1 The classical model 3915.2.1.1 The classical model as state diagram – introducing basic channel kinetics 3925.2.2 A one-site approach 3955.2.2.1 Explaining state-dependent binding – a simple electrostatic mechanism 3955.2.2.2 The relation between models assuming binding to smeared and to discrete charges 3965.2.2.3 The special case of Zn2+ – no binding in the open state 3965.2.2.4 Opposing effects of Cd2+ on hyperpolarization-activated channels 3985.3 Binding and interacting non-electrostatically with the voltage sensor (Mechanism C) 3985.3.1 Combining mechanical slowing of opening and closing with electrostatic modification of voltage sensor 4005.4 Binding to the pore – a special case of one-site binding models (Mechanism D) 4005.4.1 Voltage-dependent pore-block – adding extra gating 4015.4.2 Coupling pore block to gating 4025.4.2.1 The basic model again 4025.4.2.2 A special case – Ca2+ as necessary cofactor for closing 4035.4.2.3 Expanding the basic model – Ca2+ affecting a voltage-independent step 4045.5 Summing up 4056. Quantifying the action: comparing the metal ions 4076.1 Steady-state parameters are equally shifted 4076.2 Different metal ions cause different shifts 4086.3 Different metal ions slow gating differently 4106.4 Block of ion channels 4127. Locating the sites of action 4127.1 Fixed surface charges involved in screening 4137.2 Binding sites 4137.2.1 Group 2 ions 4147.2.2 Group 12 ions 4148. Conclusions and perspectives 4159. Appendix 41610. Acknowledgements 41811. References 418Metal ions affect ion channels either by blocking the current or by modifying the gating. In the present review we analyse the effects on the gating of voltage-gated channels. We show that the effects can be understood in terms of three main mechanisms. Mechanism A assumes screening of fixed surface charges. Mechanism B assumes binding to fixed charges and an associated electrostatic modification of the voltage sensor. Mechanism C assumes binding and an associated non-electrostatic modification of the gating. To quantify the non-electrostatic effect we introduced a slowing factor, A. A fourth mechanism (D) is binding to the pore with a consequent pore block, and could be a special case of Mechanisms B or C. A further classification considers whether the metal ion affects a single site or multiple sites. Analysing the properties of these mechanisms and the vast number of studies of metal ion effects on different voltage-gated ion channels we conclude that group 2 ions mainly affect channels by classical screening (a version of Mechanism A). The transition metals and the Zn group ions mainly bind to the channel and electrostatically modify the gating (Mechanism B), causing larger shifts of the steady-state parameters than the group 2 ions, but also different shifts of activation and deactivation curves. The lanthanides mainly bind to the channel and both electrostatically and non-electrostatically modify the gating (Mechanisms B and C). With the exception of the ether-à-go-go-like channels, most channel types show remarkably similar ion-specific sensitivities.

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Findlay, Wendy A., Gary S. Shaw, and Brian D. Sykes. "Metal ion binding by proteins." Current Opinion in Structural Biology 2, no. 1 (February 1992): 57–60. http://dx.doi.org/10.1016/0959-440x(92)90177-9.

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Findlay, Wendy A., Gary S. Shaw, and Brian D. Sykes. "Metal-ion binding by proteins." Current Biology 2, no. 3 (March 1992): 126. http://dx.doi.org/10.1016/0960-9822(92)90246-7.

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DiTusa, Charles A., Trine Christensen, Keith A. McCall, Carol A. Fierke, and Eric J. Toone. "Thermodynamics of Metal Ion Binding. 1. Metal Ion Binding by Wild-Type Carbonic Anhydrase†." Biochemistry 40, no. 18 (May 2001): 5338–44. http://dx.doi.org/10.1021/bi001731e.

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Ramyakrishna, K., and M. Sudhamani. "The metal binding potential of a dairy isolate." Journal of Water Reuse and Desalination 7, no. 4 (October 28, 2016): 429–41. http://dx.doi.org/10.2166/wrd.2016.127.

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Excess iron in water resources can lead to health hazards and problems. The ability of lactic acid bacteria to bind iron has not yet been widely studied. In the present study, sorption of iron ions from aqueous solutions onto lactic acid bacterium was determined. Elemental analyses were carried out by inductively coupled plasma optical emission spectrometry. The kinetics of Fe(III) biosorption was investigated at different initial concentrations of metal ion. The highest uptake capacity was found to be 16 mg of Fe(III) per gram of adsorbent with a contact time of 24 hr and at initial metal ion concentration of 34 mg/L. The uptake capacity of Fe(III) ion varied from 83.2 to 46.7% across the range of initial metal ion concentrations. The equilibrium data were evaluated by Langmuir and Freundlich isotherms, and were found to fit better with the latter (R2 = 0.9999). The surface morphology of the biomass and percentage of metal was characterized by using a scanning electron microscope equipped with energy dispersive X-ray spectroscopy. The functional groups on the cell wall surface of biomass involved in biosorption of heavy metals were studied by Fourier transform infrared spectroscopy spectrum.

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Baldwin, Graham S., Michael F. Bailey, B. Philip Shehan, Ioulia Sims, and Raymond S. Norton. "Tyrosine modification enhances metal-ion binding." Biochemical Journal 416, no. 1 (October 28, 2008): 77–84. http://dx.doi.org/10.1042/bj20081059.

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Tyrosine sulfation is a common modification of many proteins, and the ability to phosphorylate tyrosine residues is an intrinsic property of many growth-factor receptors. In the present study, we have utilized the peptide hormone CCK8 (cholecystokinin), which occurs naturally in both sulfated and unsulfated forms, as a model to investigate the effect of tyrosine modification on metal-ion binding. The changes in absorbance and fluorescence emission on Fe3+ binding indicated that tyrosine sulfation or phosphorylation increased the stoichiometry from 1 to 2, without greatly affecting the affinity (0.6–2.8 μM at pH 6.5). Measurement of Ca2+ binding with a Ca2+-selective electrode revealed that phosphorylated CCK8 bound two Ca2+ ions. CCK8 and sulfated CCK8 each bound only one Ca2+ ion with lower affinity. Binding of Ca2+, Zn2+ or Bi3+ to phosphorylated CCK8 did not cause any change in absorbance, but substantially increased the change in absorbance on subsequent addition of Fe3+. The results of the present study demonstrate that tyrosine modification may increase the affinity of metal-ion binding to peptides, and imply that metal ions may directly regulate many signalling pathways.

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Mauk, A. Grant, Marcia R. Mauk, Bao Lige, and Geoffrey R. Moore. "Metal ion binding to human hemopexin." Journal of Inorganic Biochemistry 96, no. 1 (July 2003): 49. http://dx.doi.org/10.1016/s0162-0134(03)80488-9.

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Mauk, Marcia R., Federico I. Rosell, Barbara Lelj-Garolla, Geoffrey R. Moore, and A. Grant Mauk. "Metal Ion Binding to Human Hemopexin†." Biochemistry 44, no. 6 (February 2005): 1864–71. http://dx.doi.org/10.1021/bi0481747.

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Dissertations / Theses on the topic "Metal ion binding"

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Satofuka, Hiroyuki. "Studies on heavy metal ion-binding peptides : Application for heavy metal ion detection and detoxification." 京都大学 (Kyoto University), 2002. http://hdl.handle.net/2433/149818.

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Sekaly, Amina L. R. "Trace metal ion binding to fulvic acids in model systems and freshwaters." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0017/NQ57625.pdf.

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Sekaly, Amina L. R. (Amina Lula R. ). Carleton University Dissertation Chemistry. "Trace metal ion binding to fulvic acids in model systems and freshwaters." Ottawa, 2000.

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Li, Zheng. "Structural Studies of Natural and Synthetic Macromolecules Stabilized by Metal Ion Binding." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1295646060.

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Prasannan, Charulata Bhaskaran. "Modulation of restriction enzyme PvuII activity by metal ion cofactors." Diss., St. Louis, Mo. : University of Missouri--St. Louis, 2009. http://etd.umsl.edu/r4461.

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Jeong, Chang-Yoon. "Modelling metal competition for adsorption sites on humic acid." Thesis, University of Nottingham, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.389363.

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Buckelew, Aurelie Lina. "Investigation of metal-ion binding in the four-way junction construct of the hairpin ribozyme." Texas A&M University, 2003. http://hdl.handle.net/1969.1/2307.

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The hairpin ribozyme is a small catalytic RNA that cleaves a phosphodiester bond. In order for cleavage to occur, the hairpin ribozyme must properly fold into its docked conformation, in which the two loops interact to form the active site. Metal ions and the four-way junction play critical roles in the stabilization of the docked conformation. The work presented in this thesis attempts to investigate the metal-ion dependence of the docking of the four-way junction construct of the hairpin ribozyme. In addition, the activity of the hairpin ribozyme in the presence of Mn2+ was observed. Initially, a four-stranded four-way junction construct of the hairpin ribozyme and a loopless mutant were characterized by native gel electrophoresis and thermal denaturation to verify ribozyme formation. A novel interaction between the sulfur of a phosphorothioate-substituted mononucleotide, such as adenosine thiomonophosphate (AMPS) or adenosine thiotrisphoshate (ATPgS), and Cd2+ has been characterized by UV-vis spectroscopy. A feature at 208 nm was identified to be a result of sulfur-to-Cd2+ transfer. The apparent binding affinities, the apparent extinction coefficients, and the binding ratios were determined for each complex.

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Reyzer, Michelle Lee. "Evaluation of metal binding interactions in host-guest chemistry using quadrupole ion trap mass spectrometry /." Full text (PDF) from UMI/Dissertation Abstracts International, 2000. http://wwwlib.umi.com/cr/utexas/fullcit?p3004364.

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Burkitt, William Ian. "Metal-binding non-covalent protein complexes studied by electrospray ionisation and Fourier transform ion cyclotron resonance mass spectrometry." Thesis, University of Warwick, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.429814.

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Zhang, Ting. "Lipid Speciation and Ion Interactions at the Air-Aqueous Interface in Atmospheric Aerosol Model Systems." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu152416015716577.

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Books on the topic "Metal ion binding"

1

Blanc, Gaillard. Biometals: Molecular structures, binding properties and applications. New York: Nova Science Publishers, 2010.

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Metal ion solvation and metal-ligand interactions. Amsterdam: Elsevier Science, 2001.

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3

Nissen, Mark Stephen. Metal ion binding to tetrameric lima bean lectin. 1985.

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Sadhu, Annamma. Saccharide and metal ion binding to concanavalin A and peanut agglutinin. 1986.

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5

Cornelis, Pierre, Wolfgang Maret, Ninian J. Blackburn, Andrea Romani, and Svetlana Lutsenko. Binding, Transport and Storage of Metal Ions in Biological Cells: Rsc. Royal Society of Chemistry, The, 2014.

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1942-, Berthon Guy, ed. Handbook of metal-ligand interactions in biological fluids. New York: Marcel Dekker, 1995.

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Bagni, Claudia, and Eric Klann. Molecular Functions of the Mammalian Fragile X Mental Retardation Protein: Insights Into Mental Retardation and Synaptic Plasticity. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199744312.003.0008.

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Chapter 8 discusses how Fragile X syndrome (FXS) is caused by the absence of the RNA-binding protein fragile X mental retardation protein (FMRP). FMRP is highly expressed in the brain and gonads, the two organs mainly affected in patients with the syndrome. Functionally, FMRP belongs to the family of RNA-binding proteins, shuttling from the nucleus to the cytoplasm, and, as shown for other RNA-binding proteins, forms large messenger ribonucleoparticles.

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8

Gaillard, Blanc, and Moreau Damien, eds. Biometals: Molecular structures, binding properties, and applications. Hauppauge, N.Y: Nova Science Publishers, 2009.

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Structure of V(H₂)n + clusters for n = 1-6. [Washington, D.C: National Aeronautics and Space Administration, 1995.

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W, Bauschlicher Charles, and United States. National Aeronautics and Space Administration., eds. Structure of V(H₂)n + clusters for n = 1-6. [Washington, D.C: National Aeronautics and Space Administration, 1995.

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Book chapters on the topic "Metal ion binding"

1

Auffinger, Pascal, Neena Grover, and Eric Westhof. "1. Metal Ion Binding to RNA." In Structural and Catalytic Roles of Metal Ions in RNA, 1–36. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849732512-00001.

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Lavery, Aidan. "Selective Metal Ion Binding by Sulphur Macrocycles." In Recent Developments in Ion Exchange, 384–95. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3449-8_38.

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Schneider, Siegfried. "Proton and metal ion binding of tetracyclines." In Tetracyclines in Biology, Chemistry and Medicine, 65–104. Basel: Birkhäuser Basel, 2001. http://dx.doi.org/10.1007/978-3-0348-8306-1_2.

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Kozlowski, Henryk, Marek Luczkowski, Daniela Valensin, and Gianni Valensin. "Metal Ion Binding Properties of Proteins Related to Neurodegeneration." In Neurodegenerative Diseases and Metal Ions, 61–87. Chichester, UK: John Wiley & Sons, Ltd, 2006. http://dx.doi.org/10.1002/0470028114.ch3.

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Morrow, Janet R., and Christopher M. Andolina. "Spectroscopic Investigations of Lanthanide Ion Binding to Nucleic Acids." In Metal Ions in Life Sciences, 171–99. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2172-2_6.

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Appoh, Francis E., and Heinz-Bernhard Kraatz. "Metal Ion Binding to Ferrocene Peptide Dendrimer Films." In Inorganic and Organometallic Macromolecules, 147–71. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-72947-3_6.

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Tan, Zhi-Jie, and Shi-Jie Chen. "3. Importance of Diffuse Metal Ion Binding to RNA." In Structural and Catalytic Roles of Metal Ions in RNA, 101–24. Cambridge: Royal Society of Chemistry, 2011. http://dx.doi.org/10.1039/9781849732512-00101.

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Luján-Upton, Hannia, and Yoshiyuki Okamoto. "Investigation of the Ion-Binding Properties of Tactic Poly(Methacrylic Acids) Using Terbium (III) Ion as a Fluorescent Probe." In Metal-Containing Polymeric Materials, 369–82. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0365-7_30.

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Devez, Aurélie, Eric Achterberg, and Martha Gledhill. "15. Metal Ion-Binding Properties of Phytochelatins and Related Ligands." In Metallothioneins and Related Chelators, 441–81. Cambridge: Royal Society of Chemistry, 2009. http://dx.doi.org/10.1039/9781847559531-00441.

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Kidokoro, Shun-ichi. "Role of Metal Ion Binding and Protonation in ATP Hydrolysis Energetics." In The Role of Water in ATP Hydrolysis Energy Transduction by Protein Machinery, 25–32. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8459-1_2.

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Conference papers on the topic "Metal ion binding"

1

Wong, Eric K. L., and Geraldine L. Richmond. "Laser excitation spectroscopic studies of metal ion binding in polymers." In AIP Conference Proceedings Volume 160. AIP, 1987. http://dx.doi.org/10.1063/1.36829.

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Nara, Masayuki, Masaru Tanokura, and Mitsuo Tasumi. "Fourier transform infrared studies on conformational changes of calmodulin induced by metal-ion binding." In Fourier Transform Spectroscopy: Ninth International Conference, edited by John E. Bertie and Hal Wieser. SPIE, 1994. http://dx.doi.org/10.1117/12.166602.

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Yap, Stephanie Hui Kit, Kok Ken Chan, Yi-Hsin Chien, and Ken-Tye Yong. "Factors Influencing Metal Binding Efficiency at Solid/Liquid Interface: An Investigation for the Prediction of Heavy Metal Ion Sensing Performance." In 2019 IEEE International Conference on Sensors and Nanotechnology (SENSORS & NANO). IEEE, 2019. http://dx.doi.org/10.1109/sensorsnano44414.2019.8940072.

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KÖhlin, A., and J. Stenflo. "HIGH AFFINITY CALCIUM BINDING TO DOMAINES OF PROTEIN C THAT ARE HOMOLOGUS TO THE EPIDERMAL GROWTH FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643645.

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In addition to γ-carboxyglutamic acid (Gla)-dependent calcium binding all of the vitamin K-dependent plasma proteins, except prothrombin, have one or two high affinity calcium binding sites that do not require the Gla residues. A common denominator among these proteins (factors IX, X, protein C, protein Z and protein S) is that they have domaines that are homologus to the epidermal growth factor (EGF) precursor. In factors VII,IX,X, protein C and in protein Z the aminoterminal of two EGF homology regions contain one residue of β-hydroxyaspartic acid (Hya) whereas in protein S the aminoterminal EGF homology region contains Hya and the three following contain one β-hydroxyasparagine residue each.In an attempt to elucidate the role of the EGF homology regions in the Gla independent calcium binding we have isolated a tryptic fragment (residue 44-138) from the light chain of human protein C. The fragment was isolated using a monoclonal antibody that recognizes a calcium ion stabilized epitope that is expressed both in intact protein C and in protein C lacking the Gla domaine.The antibody bound the isolated EGF homology region in the presence of calcium ions but not in EDTA containing buffer. A calcium ion titration showed half maximal binding at approximately 200 μM Ca2+. The metal ion induced conformational change in the isolated fragment was also studied with affinity purified rabbit antibodies against Gla domainless protein C. Antibodies that bound in the presence of calcium ions and that could be eluted with EDTA recognized the metal ion induced conformational change in the isolated EGF homology domain. Our results suggest that one or both of the EGF homology regions are involved in the Gla-independent high affinity calcium binding in the vitamin K-dependent plasma proteins.

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Jackson, Craig M., George M. Brenckle, Philip J. Hogg, and Donald J. Winzor. "EVIDENCE FOR SELF-ASSOCIATION OF PROTHROMBIN FRAGMENT 1 IN THE ABSENCE OF CALCIUM IONS: IMPLICATIONS FOR THE INTERPRETATION OF COOPERATIVITY OF CALCIUM BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643933.

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The necessity to consider the binding of metal ion by prothrombin and its fragment 1 in terms of two entirely different mechanistic models has been removed. Cooperativity of Ca+T binding to prothrombin and prothrombin fragment 1 may reflect isomerization and/or self association of the protein. Sedimentation equilibrium studies have demonstrated that both prothrombin and its fragment 1 reversibly dimerize in the absence of Ca++.Based on this pre-existing equilibrium, a model for preferential binding of Ca++ to the dimer has been found capable of accounting quantitatively for the interaction of Ca2+ with fragment 1. This phenomenon is described by the relationship r ={pkA[A][S] (1 + kA[S])p-1 + qkc X [A]2[S](1 + kc [S])q-1}/[A] in which X (1,000 M-1) denotes the association constant for the pre-existing monomer-dimer equilibrium, and p, kA (10, 100 M-1) and q, kc (20, 2,000 M-1) are the respective stoichiometries and intrinsic binding constants for the interactions of Ca++ with monomeric and dimeric fragment 1, A. There is also evidence from exclusion chromatography and sedimentation velocity experiments that different isomeric states of prothrombin and its fragment 1 exist. It is therefore proposed that a model based on co-existence of isomeric and dimeric protein states will enable quantitative differences in the Ca++-mediated responses of fragment 1 and prothrombin to be rationalized solely in terms of differences in the relative magnitudes of equilibrium constants for the same interactions in the two systems.

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Sugo, T., S. Tanabe, K. Shinoda, and M. Matsuda. "MONOCLONAL ANTIBODIES THAT RECOGNIZE Ca2+-INDUCED CONFORMER OF PROTEIN C, INDEPENDENT OF GLA RESIDUES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643644.

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Monoclonal antibodies (MCA’s) were prepared against human protein C (PC) according to Köhler & Milstein, and those that recognize the Ca2+-dependent PC conformers were screened by direct ELISA in the presence of 2 mM either CaCl2 or EDTA. Out of nine MCAߣs thus screened, five MCA's designated as HPC-1˜5, respectively, were found to react with PC in the presence of Ca2+ but not EDTA. By SDS-PAGE coupled with Western Blotting performed in the presence of 2 mM CaCl2, we found that two MCA’s HPC-1 and 2, recognized the light chain, and two others, HPC-3 and 4, recognized the heavy chain of PC. But another MCA, HPC-5 was found to react with only non-reduced antigens. Further study showed that HPC-1 and 5 failed to react with the Gla-domainless PC, i.e. PC from which the N-terminal Gla-domain of the light chain had been cleaved off by α-chymotrypsin. However, all the other three MCA's retained the reactivity with the antigen in the presence of Ca2+ even after the Gla-domain had been removed. The binding of these MCA’s to PC in the presence of Ca2+ was found to be saturable with respect to the Ca2+ concentration and the half maximal binding for each MCA was calculated to be about 0.5+mM. Moreover, many other divalent cations such as Mg2+, Mn2+ , Ba2+, Zn2+, Co2+, Sr2+, were found to substitute for Ca2+ in inducing the metal ion-dependent but Gla-domain-independent conformer of PC.Cross-reactivity to other vitamin K-aependent plasma proteins was examined by direct ELISA; HPC-2 and 3 reacted solely to PC, but HPC-1 and 4 also reacted with prothrombin and HPC-5 with both prothrombin and factor X.These findings indicated that there are two or more metal binding sites besides the Gla-domain, possibly one in the light chain and the other(s) in the heavy chain. The presence of these metal binding sites may contribute to the unique conformer of vitamin K-dependent plasma proteins including protein C.

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Brodsky, G. L., and S. P. Bajaj. "DETERMINATION OF NUMBER OF γ-CARBOXYGLUTAMIC ACID (GLA) RESIDUES INVOLVED IN FORMING THE TWO HIGH AFFINITY METAL BINDING SITES IN PROTHROMBIN AND FACTOR X." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643934.

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Prothrombin and factor X possess two high affinity and several low affinity lanthanide ion binding sites. In both proteins, the association constant of the high affinity sites is at least 50-fold greater than that of the low affinity sites. Moreover, metal bound to these high affinity sites is extremely difficult to displace. It has been proposed that one of the two high affinity sites in factor X involves Gla residues while the other involves β-hydroxyaspartic acid and no Gla residues. It is also known that ^H can be specifically incorporated into Gla residues at an acidic pH. We have determined that under nondenaturing conditions when Gla (synthetic or in proteins) is complexed to metal at pH 5.5, this specific 3H incorporation is blocked. Furthermore, we have found that β-hydroxyaspartic acid does not incorporate in the presence or absence of metal. When we incubated prothrombin or factor X (41 μM) with 3H2O in the presence of Tb3+ or Gd3+ (82 μM), we blocked 5.6 Gla residues per prothrombin and 5.5 Gla residues per factor X from 3H incorporation. Under these conditions, we calculated that >95% of the high affinity sites are occupied by metal. Thus, in prothrombin, an average of 2.8 Gla residues are involved in forming each high affinity site. If the Gla residues in factor X participate in forming only one of the two high affinity sites, then all 5.5 Gla residues blocked from incorporation must be involved in forming that site. However, this seems highly unlikely. We conclude that, as in prothrombin, both high affinity sites in factor X involve Gla residues (average 2.75/site). However, our data does not exclude the possibility of existence of a heterologous site containing both β-hydroxyaspartic acid and Gla residues.

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Murariu, Manuela. "HEAVY METAL IONS BINDING TO AMYLOID-? PEPTIDES: BIOCHEMICAL AND BIOMEDICAL IMPLICATIONS." In 18th International Multidisciplinary Scientific GeoConference SGEM2018. Stef92 Technology, 2018. http://dx.doi.org/10.5593/sgem2018/6.2/s25.049.

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Kappes, Branden B., Abbas Ebnonnasir, Suneel Kodambaka, and Cristian V. Ciobanu. "Orientation Dependent Binding Energy of Graphene on Pd(111)." In ASME 2011 International Mechanical Engineering Congress and Exposition. ASMEDC, 2011. http://dx.doi.org/10.1115/imece2011-65217.

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Graphene, a two-dimensional crystalline sheet of carbon, has generated considerable attention owing to its ultra-thin geometry, high carrier mobility and tunable band gap, with potential applications in high-performance, low-power electronics and as transparent electrodes. Since graphene–based devices require metal (or metallic) contacts, knowledge of the structural and electronic properties of the metal-graphene interfaces is essential. Previous theoretical studies of graphene-metal contacts indicate that their electronic properties depend on the metal-graphene binding energies. For example, strongly interacting metals can induce a charge transfer from or to graphene, resulting in p- or n-type doping. Here, using Pd(111) as a example substrate, we focus on understanding the influence of the orientation of graphene on its binding to the substrate.

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Jureschi, Monica. "BINDING OF HEAVY METAL IONS TO AMYLOID-? PEPTIDES: INTERACTIONS WITH NAP PEPTIDES." In 19th SGEM International Multidisciplinary Scientific GeoConference EXPO Proceedings. STEF92 Technology, 2019. http://dx.doi.org/10.5593/sgem2019/6.1/s25.075.

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Reports on the topic "Metal ion binding"

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Aluwihare, Lihini I., and Katherine Barbeau. Characterizing the Role of Metal-Binding Moieties in the Photochemistry of Chromophoric DOM in Marine Systems. Fort Belvoir, VA: Defense Technical Information Center, September 2004. http://dx.doi.org/10.21236/ada630553.

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