Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes最新文献_第4页

MARCKS, membranes, and calmodulin: kinetics of their interaction marks，膜和钙调素:它们相互作用的动力学

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00011-2

Anna Arbuzova, Diana Murray, Stuart McLaughlin

{"title":"MARCKS, membranes, and calmodulin: kinetics of their interaction","authors":"Anna Arbuzova, Diana Murray, Stuart McLaughlin","doi":"10.1016/S0304-4157(98)00011-2","DOIUrl":"10.1016/S0304-4157(98)00011-2","url":null,"abstract":"<div><p><span><span>It is well documented that membrane binding of MARCKS (Myristoylated Alanine-Rich C-Kinase Substrate) requires both hydrophobic insertion of the N-terminal myristate into the </span>bilayer<span> and electrostatic interaction of the basic effector region with acidic lipids. The structure of a membrane-bound peptide corresponding to the effector region, residues 151–175 of bovine MARCKS, was recently determined using spin-labeled peptides and EPR. The kinetics of the peptide–membrane interaction were determined from stopped-flow fluorescence measurements; the adsorption of the peptide onto phospholipid vesicles is a diffusion-limited process. Five μM Ca</span></span><sup>2+</sup><span>–calmodulin decreases the lifetime of the peptide on a 100 nm diameter 10:1 PC/PS vesicle from 0.1 s to 0.01 s by rapidly pulling the peptide off the membrane. We propose a molecular mechanism, based on previous work by M. Eigen and colleagues, by which calmodulin may remove MARCKS(151–175) from the membrane at a diffusion-limited rate. Calmodulin may also use this mechanism to remove the pseudosubstrate region from the substrate binding site of enzymes such as calmodulin kinase II and myosin light chain kinase.</span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 3","pages":"Pages 369-379"},"PeriodicalIF":0.0,"publicationDate":"1998-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00011-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20716481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 106

Hydrophobic interactions of peptides with membrane interfaces 多肽与膜界面的疏水相互作用

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00021-5

Stephen H White, William C Wimley

{"title":"Hydrophobic interactions of peptides with membrane interfaces","authors":"Stephen H White, William C Wimley","doi":"10.1016/S0304-4157(98)00021-5","DOIUrl":"10.1016/S0304-4157(98)00021-5","url":null,"abstract":"<div><p><span><span>The thermodynamic principles underlying the structural stability of membrane proteins are difficult to obtain directly from whole proteins because of intractable problems related to insolubility in the aqueous phase and extreme stability in the membrane phase. The principles must therefore be surmised from studies of the interactions of small peptides with lipid bilayers. This review is concerned with the hydrophobic interactions of such peptides with the interfacial regions of lipid bilayers. We first develop a general framework for thinking about the thermodynamics of membrane protein stability that centers on interfacial interactions and review the structural and chemical evidence that supports this interface-centered point of view. We then describe an experimentally determined whole-residue interfacial </span>hydrophobicity scale that reveals the central role of the </span>peptide bond in partitioning and folding. Finally, we consider the complexity and diversity of interfacial interactions revealed by differences between side-chain hydrophobicities determined using different classes of peptides.</p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 3","pages":"Pages 339-352"},"PeriodicalIF":0.0,"publicationDate":"1998-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00021-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20716030","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 471

Lipid polymorphism and protein–lipid interactions 脂质多态性和蛋白-脂质相互作用

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00015-X

Richard M Epand

引用次数: 332

Magainins as paradigm for the mode of action of pore forming polypeptides Magainins作为孔隙形成多肽的作用模式范例

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00014-8

Katsumi Matsuzaki

引用次数: 565

Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes1 研究多肽和蛋白质与膜相互作用的固态核磁共振方法

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00012-4

Anthony Watts

引用次数: 71

Emerging techniques for investigating molecular interactions at lipid membranes 研究脂质膜分子相互作用的新兴技术

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00020-3

Stephan Heyse , Thierry Stora , Evelyne Schmid , Jeremy H Lakey , Horst Vogel

引用次数: 92

Theoretical analysis of protein organization in lipid membranes 脂质膜中蛋白质组织的理论分析

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00022-7

Tamir Gil , John Hjort Ipsen , Ole G Mouritsen , Mads C Sabra , Maria M Sperotto , Martin J Zuckermann

{"title":"Theoretical analysis of protein organization in lipid membranes","authors":"Tamir Gil , John Hjort Ipsen , Ole G Mouritsen\u0000 , Mads C Sabra , Maria M Sperotto , Martin J Zuckermann","doi":"10.1016/S0304-4157(98)00022-7","DOIUrl":"10.1016/S0304-4157(98)00022-7","url":null,"abstract":"<div><p><span>The fundamental physical principles of the lateral organization of trans-membrane proteins and peptides as well as peripheral membrane proteins and enzymes are considered from the point of view of the lipid-bilayer membrane, its structure, dynamics, and cooperative phenomena. Based on a variety of theoretical considerations and model calculations, the nature of lipid-protein interactions is considered both for a single protein and an assembly of proteins that can lead to aggregation and </span>protein crystallization in the plane of the membrane. Phenomena discussed include lipid sorting and selectivity at protein surfaces, protein-lipid phase equilibria, lipid-mediated protein-protein interactions, wetting and capillary condensation as means of protein organization, mechanisms of two-dimensional protein crystallization, as well as non-equilibrium organization of active proteins in membranes. The theoretical findings are compared with a variety of experimental data.</p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 3","pages":"Pages 245-266"},"PeriodicalIF":0.0,"publicationDate":"1998-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00022-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20716164","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 222

Hydrophobic mismatch between proteins and lipids in membranes 膜中蛋白质和脂质之间的疏水不匹配

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-11-10 DOI: 10.1016/S0304-4157(98)00017-3

J.Antoinette Killian

{"title":"Hydrophobic mismatch between proteins and lipids in membranes","authors":"J.Antoinette Killian","doi":"10.1016/S0304-4157(98)00017-3","DOIUrl":"10.1016/S0304-4157(98)00017-3","url":null,"abstract":"<div><p><span>This review addresses the possible consequences of a mismatch in length between the hydrophobic part of membrane-spanning proteins and the hydrophobic bilayer<span> thickness for membrane structure<span> and function. Overviews are given first of the results of studies in defined model systems. These studies address effects of mismatch on protein activity, stability, orientation, aggregational state, localization, and conformation. With respect to the lipids, effects of mismatch are discussed on lipid chain order, phase transition temperature, lipid phase behavior, and microdomain formation. From these studies, it is concluded that hydrophobic mismatch can strongly affect protein and lipid organization, but that the precise consequences depend on the individual properties of the proteins and lipids. Examples of these properties include the propensity of lipids to form non-lamellar structures, the </span></span></span>amino acid composition<span> of the hydrophobic transmembrane segments of the proteins, the nature of the membrane anchoring residues, and the number of transmembrane helices. Finally, the effects of mismatch in biological membranes are discussed and its possible consequences for functional membrane processes, such as protein sorting, protein insertion, and regulation of bilayer thickness.</span></p></div>","PeriodicalId":100168,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes","volume":"1376 3","pages":"Pages 401-416"},"PeriodicalIF":0.0,"publicationDate":"1998-11-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0304-4157(98)00017-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20717018","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 556

Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules 蛋白激酶C:通过两个膜靶向模块调节蛋白质功能的范例

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-08-21 DOI: 10.1016/S0304-4157(98)00003-3

Alexandra C. Newton, Joanne E. Johnson

引用次数: 269

pH and volume homeostasis in trypanosomatids: current views and perspectives 锥虫体内的pH和体积稳态:目前的观点和观点

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes Pub Date : 1998-08-21 DOI: 10.1016/S0304-4157(98)00007-0

Lita L. Vieira

引用次数: 26