Experimental evaluation of topological parameters determining protein-folding rates

被引：78

作者：

Miller, EJ ^{[1
]}

Fischer, KF ^{[1
]}

Marqusee, S ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2002年 / 99卷 / 16期

关键词：

D O I：

10.1073/pnas.162219099

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Recent work suggests that structural topology plays a key role in determining protein-folding rates and pathways. The refolding rates of small proteins that fold without intermediates are found to correlate with simple structural parameters such as relative contact order, long-range order, or the fraction of short-range contacts. To test and evaluate the role of structural topology experimentally, a set of circular permutants of the ribosomal protein S6 from Thermus thermophilus was analyzed. Despite a wide range of relative contact order, the permuted proteins all fold with similar rates. These results suggest that alternative topological parameters may better describe the role of topology in protein-folding rates.

引用

页码：10359 / 10363

页数：5

共 47 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] PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].

ANFINSEN, CB .

SCIENCE, 1973, 181 (4096) :223-230

[3] Circular permutation and receptor insertion within green fluorescent proteins [J].

Baird, GS ;

Zacharias, DA ;

Tsien, RY .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (20) :11241-11246

[4] Protein folding dynamics: Quantitative comparison between theory and experiment [J].

Burton, RE ;

Myers, JK ;

Oas, TG .

BIOCHEMISTRY, 1998, 37 (16) :5337-5343

[5]

Chiti F, 1999, NAT STRUCT BIOL, V6, P1005

[6] Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway [J].

Clarke, J ;

Cota, E ;

Fowler, SB ;

Hamill, SJ .

STRUCTURE WITH FOLDING & DESIGN, 1999, 7 (09) :1145-1153

[7] 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

[8] Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain [J].

Doering, DS ;

Matsudaira, P .

BIOCHEMISTRY, 1996, 35 (39) :12677-12685

[9] Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism [J].

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (04) :1525-1529

[10] A rapid test for identification of autonomous folding units in proteins [J].

Fischer, KF ;

Marqusee, S .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 302 (03) :701-712

← 1 2 3 4 5 →