annurev biophys 28 1 319
➤ Gửi thông báo lỗi ⚠️ Báo cáo tài liệu vi phạmNội dung chi tiết: annurev biophys 28 1 319
annurev biophys 28 1 319
Anna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2 annurev biophys 28 1 319 28:319-365. Downloader! from www.annualreviews.org Access provided by University of Hong Kong on 08/19/16. For personal use only.MEMBRANE PROTEIN FOLDINGAND STABILITY: Physical PrinciplesStephen H. WhiteDepartment of Physiology and Biophysics, University of California at Irvine, Irvine.California 92 annurev biophys 28 1 319 697-4560; e-mail: blanco@helium.biomol.uci.eduWilliam c. WimleyDepartment of Biochemistry, Tulane University Medical Center. New Orleans,Louisiana 701annurev biophys 28 1 319
12-2739; e-mail: wwimley@mailhost.tcs.tulane.eduKEY WORDS: lipid-protein interactions, peptide-bilayer interactions, membrane-active peptides, antimicAnna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2 annurev biophys 28 1 319 ermined by the interactions of the peptide chains with each other, rhe lipid bilayer hydrocarbon core, the bilayer interface, and with water. The prediction of three-dimensional structure from sequence requires a detailed understanding of these interactions. Progress toward this objective is summari annurev biophys 28 1 319 zed in this review by means of a thermodynamic framework for describing membrane protein folding and stability. The framework includes a coherent therannurev biophys 28 1 319
modynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment ofAnna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2 annurev biophys 28 1 319 ergetics are discussed: protein binding and folding in bilayer interfaces, transmembrane helix insertion, and helix-helix interactions. The concepts of membrane protein stability that emerge provide insights to fundamental issues of protein folding.CONTENTSPERSPECTIVES AND OVERVIEW ................. annurev biophys 28 1 319 ..................................320Introduction..............................................................320Structural Features of Membrane Protannurev biophys 28 1 319
eins..................................322Assembly of Membrane Proteins and Thermodynamic Equilibrium...............3231056-8700/99/0610-0319808.003193Anna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2 annurev biophys 28 1 319 ng on 08/19/16. For personal use only.THERMODYNAMICS OF MEMBRANE PROTEINS...........................................325The Importance of Hydrogen Bonding...................................... 325Four-Step Thermodynamic Model for Membrane Protein Folding..................32sEnergetic Components of P annurev biophys 28 1 319 artitioning .....................................328Standard Transfer Free Energies...........................................330THE BILAYER MILIEU...annurev biophys 28 1 319
.........................................................331Structure of Fluid Lipid Bilayers............................................. 331PeculiarAnna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2 annurev biophys 28 1 319 e-Residue Ilydrophohicity Scales......................................339Bi layer-Induced Secondary Structure Formation............................343Theoretical Considerations................................................346Experimental Measurements................................................ annurev biophys 28 1 319 .346Till- COMPACT STATE OF MEMBRANE PRO! FINS: HELIX-HELIX INTERACTIONS.......................................................348Theoretical Consideraannurev biophys 28 1 319
tions................................................348Anna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2Anna. Rev. Biophys. Bioniol. Struct. Ì999. 28:319-65 Copyright © 1999 by Annual Reviews. All rights reservedAnnu. Rev. Biophys. Biomol. Struct. 1999.2Gọi ngay
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