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Journal articles on the topic 'Proteina transmembrana'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Ewald, Maxime, Mikihiro Shibata, Takayuki Uchihashi, Hideki Kandori, and Toshio Ando. "3F1058 OBSERVATION OF TRANSMEMBRANE PROTEIN BY HIGH SPEED ATOMIC FORCE MICROSCOPY : BACTERIORHODOPSIN D85S MUTANT, A CHLORIDE PUMP(Membrane Proteins,Oral Presentation)." Seibutsu Butsuri 52, supplement (2012): S67. http://dx.doi.org/10.2142/biophys.52.s67_3.

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2

Cronet, Philippe, Chris Sander, and Gert Vriend. "Modeling of transmembrane seven helix bundles." "Protein Engineering, Design and Selection" 6, no. 1 (1993): 59–64. http://dx.doi.org/10.1093/protein/6.1.59.

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3

Uju, Uju, Bustami Ibrahim, Wini Trilaksani, Tati Nurhayati, and Ninik Purbosari. "PROSES RECOVERY DAN PEMEKATAN BAHAN PENYEDAP DARI LIMBAH CAIR PENGOLAHAN RAJUNGAN DENGAN OSMOSIS BALIK." Jurnal Pascapanen dan Bioteknologi Kelautan dan Perikanan 4, no. 2 (2009): 177. http://dx.doi.org/10.15578/jpbkp.v4i2.450.

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Recovery dan pemekatan bahan penyedap dari limbah cair pengolahan rajungan dilakukan dengan membran osmosis balik. Tekanan transmembran (transmembrane pressure) dan suhu memberikan pengaruh signifikan terhadap fluks permeat (flux permeate). Semakin tinggi suhu maka fluks permeat akan semakin meningkat, sedangkan kenaikan tekanan transmembran hanya dapat meningkatkan fluks pada tekanan kurang dari 7.16 kPa. Sementara itu nilai rejeksi protein selama recovery tidak signifikan dipengaruhi oleh parameter operasi tekanan transmembran, suhu, dan pH. Selama pemekatan berlangsung, fluks mengalami penu

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4

Deane, Caitlin. "Taming transmembrane proteins." Nature Chemical Biology 12, no. 5 (2016): 305. http://dx.doi.org/10.1038/nchembio.2073.

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5

Cserzö, Miklos, Frank Eisenhaber, Birgit Eisenhaber, and Istvan Simon. "On filtering false positive transmembrane protein predictions." Protein Engineering, Design and Selection 15, no. 9 (2002): 745–52. http://dx.doi.org/10.1093/protein/15.9.745.

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6

Nicolas, F., M. C. Tiveron, J. Davoust, and H. Reggio. "GPI membrane anchor is determinant in intracellular accumulation of apical plasma membrane proteins in the non-polarized human colon cancer cell line HT-29 18." Journal of Cell Science 107, no. 10 (1994): 2679–89. http://dx.doi.org/10.1242/jcs.107.10.2679.

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We have compared the intracellular localization of plasma membrane proteins anchored either with a transmembrane segment or with a glycosylphosphatidylinositol moiety to estimate the effects of membrane anchor on protein segregation in the non-polarized form of the human colon cancer cell line HT-29 18. We have monitored two endogenous proteins: the carcinoembryonic antigen, a glycosylphosphatidylinositol protein and the transmembrane protein dipeptidyl peptidase IV, and two transfected proteins: the glycosylphosphatidylinositol protein Thy-1 and an engineered transmembrane form of Thy-1. Usin

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7

Ryu, Hyunil, Ahmed Fuwad, Sunhee Yoon, et al. "Biomimetic Membranes with Transmembrane Proteins: State-of-the-Art in Transmembrane Protein Applications." International Journal of Molecular Sciences 20, no. 6 (2019): 1437. http://dx.doi.org/10.3390/ijms20061437.

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In biological cells, membrane proteins are the most crucial component for the maintenance of cell physiology and processes, including ion transportation, cell signaling, cell adhesion, and recognition of signal molecules. Therefore, researchers have proposed a number of membrane platforms to mimic the biological cell environment for transmembrane protein incorporation. The performance and selectivity of these transmembrane proteins based biomimetic platforms are far superior to those of traditional material platforms, but their lack of stability and scalability rule out their commercial presen

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8

XU, EMILY W., PAUL KEARNEY, and DANIEL G. BROWN. "THE USE OF FUNCTIONAL DOMAINS TO IMPROVE TRANSMEMBRANE PROTEIN TOPOLOGY PREDICTION." Journal of Bioinformatics and Computational Biology 04, no. 01 (2006): 109–23. http://dx.doi.org/10.1142/s0219720006001722.

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Transmembrane proteins affect vital cellular functions and pathogenesis, and are a focus of drug design. It is difficult to obtain diffraction quality crystals to study transmembrane protein structure. Computational tools for transmembrane protein topology prediction fill in the gap between the abundance of transmembrane proteins and the scarcity of known membrane protein structures. Their prediction accuracy is still inadequate: TMHMM, the current state-of-the-art method, has less than 52% accuracy in topology prediction on one set of transmembrane proteins of known topology. Based on the obs

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9

Hamasaki, Naotaka, Hiroyuki Kuma, Kazuhisa Ota, Masao Sakaguchi, and Katsuyoshi Mihara. "A new concept in polytopic membrane proteins following from the study of band 3 protein." Biochemistry and Cell Biology 76, no. 5 (1998): 729–33. http://dx.doi.org/10.1139/o98-085.

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In the present communication, we introduce a novel concept in multispanning polytopic membrane proteins revealed by the study of the band 3 protein. The transmembrane domain of such proteins can be divided into three categories, that is, hydrophilic loops connecting transmembrane peptides (category 1), portions embedded by peptide-peptide interactions (category 2), and portions embedded by peptide-lipid interactions (category 3). Category 2 peptides of polytopic membrane proteins were found to stably reside in the lipid bilayer without peptide-lipid interactions that had been thought to be ess

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10

Cuthbertson, Jonathan M., Declan A. Doyle, and Mark S. P. Sansom. "Transmembrane helix prediction: a comparative evaluation and analysis." Protein Engineering, Design and Selection 18, no. 6 (2005): 295–308. http://dx.doi.org/10.1093/protein/gzi032.

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11

Tseitin, Vladimir M., and Gregory V. Nikiforovich. "Isolated transmembrane helices arranged across a membrane: computational studies." Protein Engineering, Design and Selection 12, no. 4 (1999): 305–11. http://dx.doi.org/10.1093/protein/12.4.305.

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12

Sternberg, Michael J. E. "Inter-species sequence conservation of single-spanning transmembrane regions." "Protein Engineering, Design and Selection" 4, no. 1 (1990): 45–47. http://dx.doi.org/10.1093/protein/4.1.45.

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13

Efremov, Roman G., та Gérard Vergoten. "Recognition of transmembrane α-helical segments with environmental profiles". "Protein Engineering, Design and Selection" 9, № 3 (1996): 253–63. http://dx.doi.org/10.1093/protein/9.3.253.

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14

Sugiyama, Y., N. Polulyakh, and T. Shimizu. "Identification of transmembrane protein functions by binary topology patterns." Protein Engineering Design and Selection 16, no. 7 (2003): 479–88. http://dx.doi.org/10.1093/protein/gzg068.

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15

Mravic, Marco, Hailin Hu, Zhenwei Lu та ін. "De novo designed transmembrane peptides activating the α5β1 integrin". Protein Engineering, Design and Selection 31, № 5 (2018): 181–90. http://dx.doi.org/10.1093/protein/gzy014.

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16

Martínez-Garay, Carlos A., M. Angeles Juanes, J. Carlos Igual, Ismael Mingarro, and M. Carmen Bañó. "A transmembrane serine residue in the Rot1 protein is essential for yeast cell viability." Biochemical Journal 458, no. 2 (2014): 239–49. http://dx.doi.org/10.1042/bj20131306.

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Polar residues present in transmembrane helices influence the folding or association of membrane proteins. Rot1 is a membrane protein with a single transmembrane domain. Replacement of a serine residue in the transmembrane domain by different amino acids precluded protein function, causing cell death.

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17

Kihara, D., T. Shimizu, and M. Kanehisa. "Prediction of membrane proteins based on classification of transmembrane segments." Protein Engineering Design and Selection 11, no. 11 (1998): 961–70. http://dx.doi.org/10.1093/protein/11.11.961.

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18

Bertaccini, E., and J. R. Trudell. "Predicting the transmembrane secondary structure of ligand-gated ion channels." Protein Engineering, Design and Selection 15, no. 6 (2002): 443–53. http://dx.doi.org/10.1093/protein/15.6.443.

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19

Talbert-Slagle, Kristina, Sara Marlatt, Francisco N. Barrera та ін. "Artificial Transmembrane Oncoproteins Smaller than the Bovine Papillomavirus E5 Protein Redefine Sequence Requirements for Activation of the Platelet-Derived Growth Factor β Receptor". Journal of Virology 83, № 19 (2009): 9773–85. http://dx.doi.org/10.1128/jvi.00946-09.

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ABSTRACT The bovine papillomavirus E5 protein (BPV E5) is a 44-amino-acid homodimeric transmembrane protein that binds directly to the transmembrane domain of the platelet-derived growth factor (PDGF) β receptor and induces ligand-independent receptor activation. Three specific features of BPV E5 are considered important for its ability to activate the PDGF β receptor and transform mouse fibroblasts: a pair of C-terminal cysteines, a transmembrane glutamine, and a juxtamembrane aspartic acid. By using a new genetic technique to screen libraries expressing artificial transmembrane proteins for

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20

Yoshino, Tomoko, Akiko Shimojo, Yoshiaki Maeda, and Tadashi Matsunaga. "Inducible Expression of Transmembrane Proteins on Bacterial Magnetic Particles in Magnetospirillum magneticum AMB-1." Applied and Environmental Microbiology 76, no. 4 (2009): 1152–57. http://dx.doi.org/10.1128/aem.01755-09.

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ABSTRACT Bacterial magnetic particles (BacMPs) produced by the magnetotactic bacterium Magnetospirillum magneticum AMB-1 are used for a variety of biomedical applications. In particular, the lipid bilayer surrounding BacMPs has been reported to be amenable to the insertion of recombinant transmembrane proteins; however, the display of transmembrane proteins in BacMP membranes remains a technical challenge due to the cytotoxic effects of the proteins when they are overexpressed in bacterial cells. In this study, a tetracycline-inducible expression system was developed to display transmembrane p

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21

Shafraz, Omer, Bin Xie, Soichiro Yamada, and Sanjeevi Sivasankar. "Mapping transmembrane binding partners for E-cadherin ectodomains." Proceedings of the National Academy of Sciences 117, no. 49 (2020): 31157–65. http://dx.doi.org/10.1073/pnas.2010209117.

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We combine proximity labeling and single molecule binding assays to discover transmembrane protein interactions in cells. We first screen for candidate binding partners by tagging the extracellular and cytoplasmic regions of a “bait” protein with BioID biotin ligase and identify proximal proteins that are biotin tagged on both their extracellular and intracellular regions. We then test direct binding interactions between proximal proteins and the bait, using single molecule atomic force microscope binding assays. Using this approach, we identify binding partners for the extracellular region of

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22

Andreu-Fernández, Vicente, Mónica Sancho, Ainhoa Genovés, et al. "Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes." Proceedings of the National Academy of Sciences 114, no. 2 (2016): 310–15. http://dx.doi.org/10.1073/pnas.1612322114.

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The Bcl-2 (B-cell lymphoma 2) protein Bax (Bcl-2 associated X, apoptosis regulator) can commit cells to apoptosis via outer mitochondrial membrane permeabilization. Bax activity is controlled in healthy cells by prosurvival Bcl-2 proteins. C-terminal Bax transmembrane domain interactions were implicated recently in Bax pore formation. Here, we show that the isolated transmembrane domains of Bax, Bcl-xL (B-cell lymphoma-extra large), and Bcl-2 can mediate interactions between Bax and prosurvival proteins inside the membrane in the absence of apoptotic stimuli. Bcl-2 protein transmembrane domain

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23

Bossa, Guilherme, Sean Gunderson, Rachel Downing, and Sylvio May. "Role of Transmembrane Proteins for Phase Separation and Domain Registration in Asymmetric Lipid Bilayers." Biomolecules 9, no. 8 (2019): 303. http://dx.doi.org/10.3390/biom9080303.

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It is well known that the formation and spatial correlation of lipid domains in the two apposed leaflets of a bilayer are influenced by weak lipid–lipid interactions across the bilayer’s midplane. Transmembrane proteins span through both leaflets and thus offer an alternative domain coupling mechanism. Using a mean-field approximation of a simple bilayer-type lattice model, with two two-dimensional lattices stacked one on top of the other, we explore the role of this “structural” inter-leaflet coupling for the ability of a lipid membrane to phase separate and form spatially correlated domains.

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24

Nikiforovich, G. V. "A novel, non-statistical method for predicting breaks in transmembrane helices." Protein Engineering Design and Selection 11, no. 4 (1998): 279–83. http://dx.doi.org/10.1093/protein/11.4.279.

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25

Gromiha, M. Michael. "A simple method for predicting transmembrane α helices with better accuracy". Protein Engineering, Design and Selection 12, № 7 (1999): 557–61. http://dx.doi.org/10.1093/protein/12.7.557.

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26

Boehm, J., F. Letourneur, W. Ballensiefen, D. Ossipov, C. Demolliere, and H. D. Schmitt. "Sec12p requires Rer1p for sorting to coatomer (COPI)-coated vesicles and retrieval to the ER." Journal of Cell Science 110, no. 8 (1997): 991–1003. http://dx.doi.org/10.1242/jcs.110.8.991.

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In Saccharomyces cerevisiae cells lacking the Rer1 protein (Rer1p), the type II transmembrane protein Sec12p fails to be retained in the ER. The transmembrane domain of Sec12p is sufficient to confer Rer1p-dependent ER retention to other membrane proteins. In rer1 mutants a large part of the Sec12-derived proteins can escape to the late Golgi. In contrast, rer3 mutants accumulate Sec12-derived hybrid proteins carrying early Golgi modifications. We found that rer3 mutants harbour unique alleles of the alpha-COP-encoding RET1 gene. ret1 mutants, along with other coatomer mutants, fail to retriev

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27

Gee, Heon Yung, Jiyoon Kim, and Min Goo Lee. "Unconventional secretion of transmembrane proteins." Seminars in Cell & Developmental Biology 83 (November 2018): 59–66. http://dx.doi.org/10.1016/j.semcdb.2018.03.016.

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28

Ayton, Gary S., and Gregory A. Voth. "Multiscale simulation of transmembrane proteins." Journal of Structural Biology 157, no. 3 (2007): 570–78. http://dx.doi.org/10.1016/j.jsb.2006.10.020.

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29

Bourne, H. R. "G PROTEINS IN TRANSMEMBRANE SIGNALING." Pediatric Research 33 (May 1993): S1. http://dx.doi.org/10.1203/00006450-199305001-00004.

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30

Miller, R. Tyler. "Transmembrane signalling through G proteins." Kidney International 39, no. 3 (1991): 421–29. http://dx.doi.org/10.1038/ki.1991.53.

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31

Marsh, D. "Lipid interactions with transmembrane proteins." Cellular and Molecular Life Sciences (CMLS) 60, no. 8 (2003): 1575–80. http://dx.doi.org/10.1007/s00018-003-3171-z.

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32

Chiba, Hideki, Makoto Osanai, Masaki Murata, Takashi Kojima, and Norimasa Sawada. "Transmembrane proteins of tight junctions." Biochimica et Biophysica Acta (BBA) - Biomembranes 1778, no. 3 (2008): 588–600. http://dx.doi.org/10.1016/j.bbamem.2007.08.017.

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33

Tusnády, Gábor E., László Dobson, and Peter Tompa. "Disordered regions in transmembrane proteins." Biochimica et Biophysica Acta (BBA) - Biomembranes 1848, no. 11 (2015): 2839–48. http://dx.doi.org/10.1016/j.bbamem.2015.08.002.

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34

Balda, Maria S., and Karl Matter. "Transmembrane proteins of tight junctions." Seminars in Cell & Developmental Biology 11, no. 4 (2000): 281–89. http://dx.doi.org/10.1006/scdb.2000.0177.

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35

Ilangumaran, Subburaj, Stephan Arni, Gerhild van Echten-Deckert, Bettina Borisch, and Daniel C. Hoessli. "Microdomain-dependent Regulation of Lck and Fyn Protein-Tyrosine Kinases in T Lymphocyte Plasma Membranes." Molecular Biology of the Cell 10, no. 4 (1999): 891–905. http://dx.doi.org/10.1091/mbc.10.4.891.

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Src family protein-tyrosine kinases are implicated in signaling via glycosylphosphatidylinositol (GPI)-anchored receptors. Both kinds of molecules reside in opposite leaflets of the same sphingolipid-enriched microdomains in the lymphocyte plasma membrane without making direct contact. Under detergent-free conditions, we isolated a GPI-enriched plasma membrane fraction, also containing transmembrane proteins, selectively associated with sphingolipid microdomains. Nonionic detergents released the transmembrane proteins, yielding core sphingolipid microdomains, limited amounts of which could als

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36

Roy Choudhury, Amrita, Nikolay Zhukov, and Marjana Novič. "Mathematical Characterization of Protein Transmembrane Regions." Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/607830.

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Graphical bioinformatics has paved a unique way of mathematical characterization of proteins and proteomic maps. The graphics representations and the corresponding mathematical descriptors have proved to be useful and have provided unique solutions to problems related to identification, comparisons, and analyses of protein sequences and proteomics maps. Based on sequence information alone, these descriptors are independent from physiochemical properties of amino acids and evolutionary information. In this work, we have presented invariants from amino acid adjacency matrix and decagonal isometr

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37

Ye, Jin. "Transcription factors activated through RIP (regulated intramembrane proteolysis) and RAT (regulated alternative translocation)." Journal of Biological Chemistry 295, no. 30 (2020): 10271–80. http://dx.doi.org/10.1074/jbc.rev120.012669.

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Transmembrane proteins are membrane-anchored proteins whose topologies are important for their functions. These properties enable regulation of certain transmembrane proteins by regulated intramembrane proteolysis (RIP) and regulated alternative translocation (RAT). RIP enables a protein fragment of a transmembrane precursor to function at a new location, and RAT leads to an inverted topology of a transmembrane protein by altering the direction of its translocation across membranes during translation. RIP mediated by site-1 protease (S1P) and site-2 protease (S2P) is involved in proteolytic ac

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38

Froquet, Romain, Marion le Coadic, Jackie Perrin, Nathalie Cherix, Sophie Cornillon, and Pierre Cosson. "TM9/Phg1 and SadA proteins control surface expression and stability of SibA adhesion molecules inDictyostelium." Molecular Biology of the Cell 23, no. 4 (2012): 679–86. http://dx.doi.org/10.1091/mbc.e11-04-0338.

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TM9 proteins form a family of conserved proteins with nine transmembrane domains essential for cellular adhesion in many biological systems, but their exact role in this process remains unknown. In this study, we found that genetic inactivation of the TM9 protein Phg1A dramatically decreases the surface levels of the SibA adhesion molecule in Dictyostelium amoebae. This is due to a decrease in sibA mRNA levels, in SibA protein stability, and in SibA targeting to the cell surface. A similar phenotype was observed in cells devoid of SadA, a protein that does not belong to the TM9 family but also

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39

Lal, Mark, and Michael Caplan. "Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions." Physiology 26, no. 1 (2011): 34–44. http://dx.doi.org/10.1152/physiol.00028.2010.

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Intramembrane cleavage of transmembrane proteins is a fundamental cellular process. Several enzymes capable of releasing domains of integral membrane proteins have been described. Transmembrane protein proteolytic cleavage is regulated and involved not only in degrading membrane spanning segments but also in generating messengers that elicit biological responses. This review examines the role of the released functional protein domain in signaling mechanisms regulating an array of cellular and physiological processes.

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40

Pasquier, C., and S. J. Hamodrakas. "An hierarchical artificial neural network system for the classification of transmembrane proteins." Protein Engineering, Design and Selection 12, no. 8 (1999): 631–34. http://dx.doi.org/10.1093/protein/12.8.631.

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41

Otzen, D. E. "Mapping the folding pathway of the transmembrane protein DsbB by protein engineering." Protein Engineering Design and Selection 24, no. 1-2 (2010): 139–49. http://dx.doi.org/10.1093/protein/gzq079.

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42

Marlatt, S. A., Y. Kong, T. J. Cammett, G. Korbel, J. P. Noonan, and D. DiMaio. "Construction and maintenance of randomized retroviral expression libraries for transmembrane protein engineering." Protein Engineering Design and Selection 24, no. 3 (2010): 311–20. http://dx.doi.org/10.1093/protein/gzq112.

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43

Pralle, A., P. Keller, E. L. Florin, K. Simons, and J. K. H. Hörber. "Sphingolipid–Cholesterol Rafts Diffuse as Small Entities in the Plasma Membrane of Mammalian Cells." Journal of Cell Biology 148, no. 5 (2000): 997–1008. http://dx.doi.org/10.1083/jcb.148.5.997.

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To probe the dynamics and size of lipid rafts in the membrane of living cells, the local diffusion of single membrane proteins was measured. A laser trap was used to confine the motion of a bead bound to a raft protein to a small area (diam ≤ 100 nm) and to measure its local diffusion by high resolution single particle tracking. Using protein constructs with identical ectodomains and different membrane regions and vice versa, we demonstrate that this method provides the viscous damping of the membrane domain in the lipid bilayer. When glycosylphosphatidylinositol (GPI) -anchored and transmembr

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44

Topham, Christopher M., Lionel Moulédous, and Jean-Claude Meunier. "On the spatial disposition of the fifth transmembrane helix and the structural integrity of the transmembrane binding site in the opioid and ORL1 G protein-coupled receptor family." Protein Engineering, Design and Selection 13, no. 7 (2000): 477–90. http://dx.doi.org/10.1093/protein/13.7.477.

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45

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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46

Babst, Markus. "Quality control at the plasma membrane: One mechanism does not fit all." Journal of Cell Biology 205, no. 1 (2014): 11–20. http://dx.doi.org/10.1083/jcb.201310113.

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The plasma membrane quality control system of eukaryotic cells is able to recognize and degrade damaged cell surface proteins. Recent studies have identified two mechanisms involved in the recognition of unfolded transmembrane proteins. One system uses chaperones to detect unfolded cytoplasmic domains of transmembrane proteins, whereas the second mechanism relies on an internal quality control system of the protein, which can trigger degradation when the protein deviates from the folded state. Both quality control mechanisms are key to prevent proteotoxic effects at the cell surface and to ens

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47

Heim, Erin N., Jez L. Marston, Ross S. Federman, et al. "Biologically active LIL proteins built with minimal chemical diversity." Proceedings of the National Academy of Sciences 112, no. 34 (2015): E4717—E4725. http://dx.doi.org/10.1073/pnas.1514230112.

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We have constructed 26-amino acid transmembrane proteins that specifically transform cells but consist of only two different amino acids. Most proteins are long polymers of amino acids with 20 or more chemically distinct side-chains. The artificial transmembrane proteins reported here are the simplest known proteins with specific biological activity, consisting solely of an initiating methionine followed by specific sequences of leucines and isoleucines, two hydrophobic amino acids that differ only by the position of a methyl group. We designate these proteins containing leucine (L) and isoleu

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48

Li, Shanshan, Huoqing Luo, Ronghui Lou, et al. "Multiregional profiling of the brain transmembrane proteome uncovers novel regulators of depression." Science Advances 7, no. 30 (2021): eabf0634. http://dx.doi.org/10.1126/sciadv.abf0634.

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Transmembrane proteins play vital roles in mediating synaptic transmission, plasticity, and homeostasis in the brain. However, these proteins, especially the G protein–coupled receptors (GPCRs), are underrepresented in most large-scale proteomic surveys. Here, we present a new proteomic approach aided by deep learning models for comprehensive profiling of transmembrane protein families in multiple mouse brain regions. Our multiregional proteome profiling highlights the considerable discrepancy between messenger RNA and protein distribution, especially for region-enriched GPCRs, and predicts an

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49

Ortells, M. O., G. E. Barrantes, C. Wood, G. G. Lunt, and F. J. Barrantes. "Molecular modelling of the nicotinic acetylcholine receptor transmembrane region in the open state." Protein Engineering Design and Selection 10, no. 5 (1997): 511–17. http://dx.doi.org/10.1093/protein/10.5.511.

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50

Braun, Volkmar, and Christina Herrmann. "Docking of the Periplasmic FecB Binding Protein to the FecCD Transmembrane Proteins in the Ferric Citrate Transport System of Escherichia coli." Journal of Bacteriology 189, no. 19 (2007): 6913–18. http://dx.doi.org/10.1128/jb.00884-07.

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ABSTRACT Citrate-mediated iron transport across the cytoplasmic membrane is catalyzed by an ABC transporter that consists of the periplasmic binding protein FecB, the transmembrane proteins FecC and FecD, and the ATPase FecE. Salt bridges between glutamate residues of the binding protein and arginine residues of the transmembrane proteins are predicted to mediate the positioning of the substrate-loaded binding protein on the transmembrane protein, based on the crystal structures of the ABC transporter for vitamin B12, consisting of the BtuF binding protein and the BtuCD transmembrane proteins

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