Solvation Dynamics of Model Peptides Probed by Terahertz Spectroscopy. Observation of the Onset of Collective Network Motions

被引：113

作者：

Born, Benjamin ^{[1
]}

Weingaertner, Hermann ^{[1
]}

Bruendermann, Erik ^{[1
]}

Havenith, Martina ^{[1
]}

机构：

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

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 10期

关键词：

HYDRATION DYNAMICS; WATER DYNAMICS; SHELL;

D O I：

10.1021/ja808997y

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We have studied the solvation of model peptides at low hydration levels by terahertz absorption spectroscopy. We have recorded the concentration-dependent terahertz absorption coefficients of A acetylglycine-amide (NAGA), N-acetyl-glycine-methylamide (NAGMA), N-acetyl-leucine-amide (NALA), N-acetyl-leucine-methylamide (NALMA), and N-acetyl-tryptophan-amide (NATA) in aqueous solution. We find a dramatic decrease in the THz absorption, if the number of water molecules per solute is less than 18-20. This change is taken as a signature for the breakdown of peptide-water network motions, which supports the hypothesis that a minimum number of hydration waters is required to activate these motions. This is well below a monolayer coverage of the model peptides. It is interesting to note that the required hydration level corresponds to the number of water molecules which are required for biological functionality.

引用

页码：3752 / 3755

页数：4

共 22 条

[1] Water as an active constituent in cell biology [J].

Ball, Philip .

CHEMICAL REVIEWS, 2008, 108 (01) :74-108

[2] New p-Ge THz laser spectrometer for the study of solutions:: THz absorption spectroscopy of water -: art. no. 063110 [J].

Bergner, A ;

Heugen, U ;

Bründermann, E ;

Schwaab, G ;

Havenith, M ;

Chamberlin, DR ;

Haller, EE .

REVIEW OF SCIENTIFIC INSTRUMENTS, 2005, 76 (06)

[3] The terahertz dance of water with the proteins: the effect of protein flexibility on the dynamical hydration shell of ubiquitin [J].

Born, Benjamin ;

Kim, Seung Joong ;

Ebbinghaus, Sinion ;

Gruebele, Martin ;

Havenith, Martina .

FARADAY DISCUSSIONS, 2009, 141 :161-173

[4] Dielectric modulation of biological water -: art. no. 228104 [J].

Despa, F ;

Fernández, A ;

Berry, RS .

PHYSICAL REVIEW LETTERS, 2004, 93 (22) :228104-1

[5] 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

[6] 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

[7] 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

[8] Protein Dynamical Transition Does Not Require Protein Structure [J].

He, Yunfen ;

Ku, Pei I. ;

Knab, J. R. ;

Chen, J. Y. ;

Markelz, A. G. .

PHYSICAL REVIEW LETTERS, 2008, 101 (17)

[9] Differences in hydration structure near hydrophobic and hydrophilic amino acids [J].

HeadGordon, T ;

Sorenson, JM ;

Pertsemlidis, A ;

Glaeser, RM .

BIOPHYSICAL JOURNAL, 1997, 73 (04) :2106-2115

[10] 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

← 1 2 3 →