Rapid mixing methods for exploring the kinetics of protein folding

被引：54

作者：

Roder, H

Maki, K

Cheng, H

Shastry, MCR

机构：

[1] Fox Chase Canc Ctr, Div Basic Sci, Philadelphia, PA 19111 USA

[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

METHODS | 2004年 / 34卷 / 01期

关键词：

ultrafast mixing; stopped-flow; continuous-flow; fluorescence; NMR;

D O I：

10.1016/j.ymeth.2004.03.003

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Information on the time-dependence of molecular species is critical for elucidating reaction mechanisms in chemistry and biology. Rapid flow experiments involving turbulent mixing of two or more solutions continue to be the main source of kinetic information on protein folding and other biochemical processes, such as ligand binding and enzymatic reactions. Recent advances in mixer design and detection methods have opened a new window for exploring conformational changes in proteins on the microsecond time scale. These developments have been especially important for exploring early stages of protein folding. (C) 2004 Elsevier Inc. All rights reserved.

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收藏

页码：15 / 27

页数：13

相关论文

共 87 条

[11] Submillisecond protein folding kinetics studied by ultrarapid mixing [J].

Chan, CK ;

Hu, Y ;

Takahashi, S ;

Rousseau, DL ;

Eaton, WA ;

Hofrichter, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (05) :1779-1784

[12]

CHANCE B, 1964, RAPID MIXING SAMPLIN

[13] Toward understanding tryptophan fluorescence in proteins [J].

Chen, Y ;

Barkley, MD .

BIOCHEMISTRY, 1998, 37 (28) :9976-9982

[14] Probing the folding pathway of a β-clam protein with single-tryptophan constructs [J].

Clark, PL ;

Weston, BF ;

Gierasch, LM .

FOLDING & DESIGN, 1998, 3 (05) :401-412

[15] Kinetic intermediates in the formation of the cytochrome c molten globule [J].

Colon, W ;

Roder, H .

NATURE STRUCTURAL BIOLOGY, 1996, 3 (12) :1019-1025

[16] Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding [J].

Colon, W ;

Elove, GA ;

Wakem, LP ;

Sherman, F ;

Roder, H .

BIOCHEMISTRY, 1996, 35 (17) :5538-5549

[17] Identification of the predominant non-native histidine ligand in unfolded cytochrome c [J].

Colon, W ;

Wakem, LP ;

Sherman, F ;

Roder, H .

BIOCHEMISTRY, 1997, 36 (41) :12535-12541

[18] EPR-detected folding kinetics of externally located cysteine-directed spin-labeled mutants of iso-1-cytochrome c [J].

Deweerd, K ;

Grigoryants, V ;

Sun, YH ;

Fetrow, JS ;

Scholes, CP .

BIOCHEMISTRY, 2001, 40 (51) :15846-15855

[19] Fast kinetics and mechanisms in protein folding [J].

Eaton, WA ;

Muñoz, V ;

Hagen, SJ ;

Jas, GS ;

Lapidus, LJ ;

Henry, ER ;

Hofrichter, J .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 2000, 29 :327-359

[20]

Eftink MR, 1997, METHOD ENZYMOL, V278, P258

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