Evidence of Coupling between the Motions of Water and Peptides
Journal article, 2016
Studies of protein dynamics at low temperatures are generally performed on hydrated powders and not in biologically realistic solutions of water because of water crystallization. However, here we avoid the problem of crystallization by reducing the size of the biomolecules. We have studied oligomers of the amino acid L-lysine, fully dissolved in water, and our dielectric relaxation data show that the glass transition-related dynamics of the oligomers is determined by the water dynamics, in a way similar to that previously observed for solvated proteins. This implies that the crucial role of water for protein dynamics can be extended to other types of macromolecular systems, where water is also able to determine their conformational fluctuations. Using the energy landscape picture of macromolecules, the thermodynamic criterion for such solvent-slaved macromolecular motions may be that the macromolecules need the entropy contribution from the solvent to overcome the enthalpy barriers between different conformational substates.
WATER
V106
SUPERCOOLED
PROTEIN DYNAMICS
SOLVENT
HYDRATION WATER
P5129
Materials Science
BOVINE SERUM-ALBUMIN
Chemistry
Molecular & Chemical
Physics
CONFINED WATER
RELAXATION
Atomic
GLASS-TRANSITION
LYSINE
ATES OF AMERICA
Nanoscience & Nanotechnology
MYOGLOBIN
Physical
Multidisciplinary
Author
S. Cerveny
Centro de Física de Materiales (CSIC-UPV/EHU)
Donostia International Physics Center
I. Combarro-Palacios
Centro de Física de Materiales (CSIC-UPV/EHU)
Jan Swenson
Chalmers, Physics, Condensed Matter Physics
Journal of Physical Chemistry Letters
1948-7185 (eISSN)
Vol. 7 20 4093-4098Driving Forces
Sustainable development
Areas of Advance
Materials Science
Subject Categories
Condensed Matter Physics
DOI
10.1021/acs.jpclett.6b01864