Smaller and faster:: The 20-residue Trp-cage protein folds in 4 μs

被引:293
作者
Qiu, LL [1 ]
Pabit, SA [1 ]
Roitberg, AE [1 ]
Hagen, SJ [1 ]
机构
[1] Univ Florida, Dept Phys, Chem Dept & Quantum Theory Project, Gainesville, FL 32611 USA
关键词
D O I
10.1021/ja0279141
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We have used laser temperature jump spectroscopy to measure the folding speed of the 20-residue Trp-cage, the smallest polypeptide known to exhibit truly cooperative folding behavior. The observed folding time (4 μs at room temperature) makes this not only the smallest foldable protein, but also the fastest, with a folding speed that exceeds contact-order predictions and approaches anticipated diffusional "speed limits" for protein folding. Copyright © 2002 American Chemical Society.
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收藏
页码:12952 / 12953
页数:2
相关论文
共 22 条
[1]   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
[2]   The energy landscape of a fast-folding protein mapped by Ala->Gly substitutions [J].
Burton, RE ;
Huang, GS ;
Daugherty, MA ;
Calderone, TL ;
Oas, TG .
NATURE STRUCTURAL BIOLOGY, 1997, 4 (04) :305-310
[3]   Fast events in protein folding: The time evolution of primary processes [J].
Callender, RH ;
Dyer, RB ;
Gilmanshin, R ;
Woodruff, WH .
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, 1998, 49 :173-202
[4]   Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution [J].
Duan, Y ;
Kollman, PA .
SCIENCE, 1998, 282 (5389) :740-744
[5]   Ultrafast folding of WW domains without structured aromatic clusters in the denatured state [J].
Ferguson, N ;
Johnson, CM ;
Macias, M ;
Oschkinat, H ;
Fersht, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (23) :13002-13007
[6]   Mini-proteins Trp the light fantastic [J].
Gellman, SH ;
Woolfson, DN .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (06) :408-410
[7]   Diffusion-limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding [J].
Hagen, SJ ;
Hofrichter, J ;
Szabo, A ;
Eaton, WA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (21) :11615-11617
[8]   Rate of intrachain contact formation in an unfolded protein: Temperature and denaturant effects [J].
Hagen, SJ ;
Carswell, CW ;
Sjolander, EM .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 305 (05) :1161-1171
[9]   Application of the diffusion-collision model to the folding of three-helix bundle proteins [J].
Islam, SA ;
Karplus, M ;
Weaver, DL .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 318 (01) :199-215
[10]   The folding mechanism of a β-sheet:: The WW domain [J].
Jäger, M ;
Nguyen, H ;
Crane, JC ;
Kelly, JW ;
Gruebele, M .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (02) :373-393