Dynamic transition in tRNA is solvent induced

被引:97
作者
Caliskan, G
Briber, RM
Thirumalai, D
Garcia-Sakai, V
Woodson, SA
Sokolov, AP [1 ]
机构
[1] Univ Akron, Dept Polymer Sci, Akron, OH 44325 USA
[2] Johns Hopkins Univ, Dept Biophys, Baltimore, MD 21218 USA
[3] Univ Maryland, Dept Mat Sci & Engn, IPST, College Pk, MD 20472 USA
[4] NIST, Ctr Neutron Res, Gaithersburg, MD 20899 USA
[5] Univ Maryland, Biophys Program, IPST, College Pk, MD USA
关键词
D O I
10.1021/ja056444i
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Dynamics of tRNA was studied using neutron scattering spectroscopy. Despite vast differences in the architecture and backbone structure of proteins and RNA, hydrated tRNA undergoes the dynamic transition at the same temperature as hydrated lysozyme. The similarity of the dynamic transition in RNA and proteins supports the idea that it is solvent induced. Because tRNA essentially has no methyl groups, the results also suggest that methyl groups are not the main contributor of the dynamic transition in biological macromolecules. However, they may explain strong differences in the dynamics of tRNA and lysozyme observed at low temperatures. Copyright © 2006 American Chemical Society.
引用
收藏
页码:32 / 33
页数:2
相关论文
共 22 条
[1]   Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature [J].
Cordone, L ;
Ferrand, M ;
Vitrano, E ;
Zaccai, G .
BIOPHYSICAL JOURNAL, 1999, 76 (02) :1043-1047
[2]   Internal dynamics and protein-matrix coupling in trehalose-coated proteins [J].
Cordone, L ;
Cottone, G ;
Giuffrida, S ;
Palazzo, G ;
Venturoli, G ;
Viappiani, C .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2005, 1749 (02) :252-281
[3]   DYNAMICAL TRANSITION OF MYOGLOBIN REVEALED BY INELASTIC NEUTRON-SCATTERING [J].
DOSTER, W ;
CUSACK, S ;
PETRY, W .
NATURE, 1989, 337 (6209) :754-756
[4]   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
[5]   THERMAL MOTIONS AND FUNCTION OF BACTERIORHODOPSIN IN PURPLE MEMBRANES - EFFECTS OF TEMPERATURE AND HYDRATION STUDIED BY NEUTRON-SCATTERING [J].
FERRAND, M ;
DIANOUX, AJ ;
PETRY, W ;
ZACCAI, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (20) :9668-9672
[6]   RELAXATION PROCESSES IN SUPERCOOLED LIQUIDS [J].
GOTZE, W ;
SJOGREN, L .
REPORTS ON PROGRESS IN PHYSICS, 1992, 55 (03) :241-376
[7]  
GOTZE W, 1995, T THEORY STAT PHYS, V24
[8]   Temperature dependence of protein dynamics: Computer simulation analysis of neutron scattering properties [J].
Hayward, JA ;
Smith, JC .
BIOPHYSICAL JOURNAL, 2002, 82 (03) :1216-1225
[9]   Microscopic origins of entropy, heat capacity and the glass transition in proteins [J].
Lee, AL ;
Wand, AJ .
NATURE, 2001, 411 (6836) :501-504
[10]   Heme-solvent coupling: A Mossbauer study of myoglobin in sucrose [J].
Lichtenegger, H ;
Doster, W ;
Kleinert, T ;
Birk, A ;
Sepiol, B ;
Vogl, G .
BIOPHYSICAL JOURNAL, 1999, 76 (01) :414-422