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.
P5129
SOLVENT
GLASS-TRANSITION
Nanoscience & Nanotechnology
Chemistry
ATES OF AMERICA
MYOGLOBIN
LYSINE
CONFINED WATER
Physics
WATER
BOVINE SERUM-ALBUMIN
Physical
PROTEIN DYNAMICS
Multidisciplinary
Materials Science
HYDRATION WATER
RELAXATION
V106
Molecular & Chemical
SUPERCOOLED
Atomic
Author
S. Cerveny
Donostia International Physics Center
Spanish National Research Council (CSIC)
I. Combarro-Palacios
Spanish National Research Council (CSIC)
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 (SSIF 2011)
Condensed Matter Physics
DOI
10.1021/acs.jpclett.6b01864