Local versus nonlocal interactions in protein folding and stability - An experimentalist's point of view

被引:78
作者
Munoz, V [1 ]
Serrano, L [1 ]
机构
[1] EUROPEAN MOL BIOL LAB,D-69012 HEIDELBERG,GERMANY
来源
FOLDING & DESIGN | 1996年 / 1卷 / 04期
关键词
ALPHA-HELIX STABILITY; SIDE-CHAIN INTERACTIONS; HYDROPHOBIC-STAPLE MOTIF; AMINO-ACIDS; SECONDARY STRUCTURE; PEPTIDE-FRAGMENTS; CAPPING BOX; THERMODYNAMIC SCALE; FORMING TENDENCIES; POLYPEPTIDE-CHAIN;
D O I
10.1016/S1359-0278(96)00036-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
One of the classic important issues in protein folding and stability is the relative roles of noncovalent short-range (local) and long-range (nonlocal) interactions, Interest in this topic has been reinforced by recent developments in the analytical theory of protein folding and in lattice-based computer simulations. During the past few years, a wealth of experimental information relevant to this issue has been accumulating. In this review, we focus specifically on experimental aspects, discussing some general ideas that arise from the results obtained by many different groups using a variety of approaches, We also discuss a new experimental strategy that allows us to engineer the contribution of local interactions, and we discuss the first results obtained. (C) Current Biology Ltd
引用
收藏
页码:R71 / R77
页数:7
相关论文
共 80 条
[1]   IMPACT OF LOCAL AND NONLOCAL INTERACTIONS ON THERMODYNAMICS AND KINETICS OF PROTEIN-FOLDING [J].
ABKEVICH, VI ;
GUTIN, AM ;
SHAKHNOVICH, EI .
JOURNAL OF MOLECULAR BIOLOGY, 1995, 252 (04) :460-471
[2]  
Anfinsen C B, 1975, Adv Protein Chem, V29, P205, DOI 10.1016/S0065-3233(08)60413-1
[3]   RULES FOR ALPHA-HELIX TERMINATION BY GLYCINE [J].
AURORA, R ;
SRINIVASAN, R ;
ROSE, GD .
SCIENCE, 1994, 264 (5162) :1126-1130
[4]   HYDROGEN-BOND STRENGTH AND BETA-SHEET PROPENSITIES - THE ROLE OF A SIDE-CHAIN BLOCKING EFFECT [J].
BAI, YW ;
ENGLANDER, SW .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1994, 18 (03) :262-266
[5]   DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF 6 AMINO-ACID SUBSTITUTIONS AT THR 59 [J].
BELL, JA ;
BECKTEL, WJ ;
SAUER, U ;
BAASE, WA ;
MATTHEWS, BW .
BIOCHEMISTRY, 1992, 31 (14) :3590-3596
[6]   STRUCTURAL BASIS OF AMINO-ACID ALPHA-HELIX PROPENSITY [J].
BLABER, M ;
ZHANG, XJ ;
MATTHEWS, BW .
SCIENCE, 1993, 260 (5114) :1637-1640
[7]  
BLANCO FJ, 1995, EUR J BIOCHEM, V230, P634
[8]   THE ROLE OF TURNS IN THE STRUCTURE OF AN ALPHA-HELICAL PROTEIN [J].
BRUNET, AP ;
HUANG, ES ;
HUFFINE, ME ;
LOEB, JE ;
WELTMAN, RJ ;
HECHT, MH .
NATURE, 1993, 364 (6435) :355-358
[9]   FUNNELS, PATHWAYS, AND THE ENERGY LANDSCAPE OF PROTEIN-FOLDING - A SYNTHESIS [J].
BRYNGELSON, JD ;
ONUCHIC, JN ;
SOCCI, ND ;
WOLYNES, PG .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 1995, 21 (03) :167-195
[10]   H-1-NMR PARAMETERS OF THE COMMON AMINO-ACID RESIDUES MEASURED IN AQUEOUS-SOLUTIONS OF THE LINEAR TETRAPEPTIDES H-GLY-GLY-X-L-ALA-OH [J].
BUNDI, A ;
WUTHRICH, K .
BIOPOLYMERS, 1979, 18 (02) :285-297