Real-time detection of protein-water dynamics upon protein folding by terahertz absorption spectroscopy

被引：121

作者：

Kim, Seting Joong

Born, Benjamin ^{[3
]}

Havenith, Martina ^{[3
]}

Gruebele, Martin ^{[1
,2
]}

机构：

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

[2] Univ Illinois, Dept Biophys & Computat Biol, Urbana, IL 61801 USA

[3] Ruhr Univ Bochum, Lehrstuhl Phys Chem 2, D-44780 Bochum, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 34期

关键词：

circular dichroism; fluorescence; protein folding; secondary structure; terahertz spectroscopy;

D O I：

10.1002/anie.200802281

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Take a look around: Kinetic terahertz absorption (KITA) spectroscopy has been used to monitor the attenuation and phase shift of a terahertz electric field transmitted through a protein during refolding. Comparison with data from fluorescence, circular dichroism, and small angle X-ray scattering shows that KITA monitors rearrangements of the hydration water-protein interactions during early collapse and secondary structure formation. (Figure Presented). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

收藏

页码：6486 / 6489

页数：4

相关论文

共 21 条

[1]

BORN B, 2008, FARADAY DIS IN PRESS

[2]

Dexheimer S. L., 2007, TERAHERTZ SPECTROSCO

[3] Protein sequence- and pH-dependent hydration probed by terahertz spectroscopy [J].

Ebbinghaus, Simon ;

Kim, Seung Joong ;

Heyden, Matthias ;

Yu, Xin ;

Gruebele, Martin ;

Leitner, David M. ;

Havenith, Martina .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (08) :2374-2375

[4] An extended dynamical hydration shell around proteins [J].

Ebbinghaus, Simon ;

Kim, Seung Joong ;

Heyden, Matthias ;

Yu, Xin ;

Heugen, Udo ;

Gruebele, Martin ;

Leitner, David M. ;

Havenith, Martina .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (52) :20749-20752

[5] What causes hyperfluorescence:: Folding intermediates or conformationally flexible native states? [J].

Ervin, J ;

Larios, E ;

Osváth, S ;

Schulten, K ;

Gruebele, M .

BIOPHYSICAL JOURNAL, 2002, 83 (01) :473-483

[6] Slaving: Solvent fluctuations dominate protein dynamics and functions [J].

Fenimore, PW ;

Frauenfelder, H ;

McMahon, BH ;

Parak, FG .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (25) :16047-16051

[7] Terahertz radiation from bacteriorhodopsin reveals correlated primary electron and proton transfer processes [J].

Groma, G. I. ;

Hebling, J. ;

Kozma, I. Z. ;

Varo, G. ;

Hauer, J. ;

Kuhl, J. ;

Riedle, E. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (19) :6888-6893

[8] Solute-induced retardation of water dynamics probed directly by terahertz spectroscopy [J].

Heugen, U. ;

Schwaab, G. ;

Bruendermann, E. ;

Heyden, M. ;

Yu, X. ;

Leitner, D. M. ;

Havenith, M. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (33) :12301-12306

[9] Water contributes actively to the rapid crossing of a protein unfolding barrier [J].

Jacob, MH ;

Saudan, C ;

Holtermann, G ;

Martin, A ;

Perl, D ;

Merbach, AE ;

Schmid, FX .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 318 (03) :837-845

[10] FOLDING AND STABILITY OF A TRYPTOPHAN-CONTAINING MUTANT OF UBIQUITIN [J].

KHORASANIZADEH, S ;

PETERS, ID ;

BUTT, TR ;

RODER, H .

BIOCHEMISTRY, 1993, 32 (27) :7054-7063