Protein folding: the free energy surface

被引：103

作者：

Gruebele, M

机构：

[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Phys, Urbana, IL 61801 USA

[3] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2002年 / 12卷 / 02期

关键词：

D O I：

10.1016/S0959-440X(02)00304-4

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：

Quantitative models and experiments are revealing how the folding free energy surface of a protein is sculpted by sequence and environment. The sometimes conflicting demands of folding, structure and function determine which folding pathways, if any, dominate. Recent advances include experimental estimates of diffusive barrier-crossing times, the observation of ultrafast folders amenable to full-atom simulation, the use of thermodynamic tuning and nonconservative mutations to probe 'hidden' parts of the free energy surface, and a complete microscopic theory of folding.

引用

收藏

页码：161 / 168

页数：8

相关论文

共 57 条

[1] Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures [J].

Alm, E ;

Baker, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (20) :11305-11310

[2] A surprising simplicity to protein folding [J].

Baker, D .

NATURE, 2000, 405 (6782) :39-42

[3] The speed limit for protein folding measured by triplet-triplet energy transfer [J].

Bieri, O ;

Wirz, J ;

Hellrung, B ;

Schutkowski, M ;

Drewello, M ;

Kiefhaber, T .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (17) :9597-9601

[4] A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding [J].

Bieri, O ;

Wildegger, G ;

Bachmann, A ;

Wagner, C ;

Kiefhaber, T .

BIOCHEMISTRY, 1999, 38 (38) :12460-12470

[5] Reaction coordinates of biomolecular isomerization [J].

Bolhuis, PG ;

Dellago, C ;

Chandler, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (11) :5877-5882

[6]

Capaldi AP, 2001, NAT STRUCT BIOL, V8, P68

[7] Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin [J].

Cavagnero, S ;

Dyson, HJ ;

Wright, PE .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (01) :269-282

[8] What is the role of non-native intermediates of β-lactoglobulin in protein folding? [J].

Chikenji, G ;

Kikuchi, M .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (26) :14273-14277

[9] Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins [J].

Clementi, C ;

Nymeyer, H ;

Onuchic, JN .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 298 (05) :937-953

[10] Mapping the transition state of the WW domain β-sheet [J].

Crane, JC ;

Koepf, EK ;

Kelly, JW ;

Gruebele, M .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 298 (02) :283-292

← 1 2 3 4 5 6 →