An effective environmental force constant is introduced to quantify the molecular resilience
(or its opposite,“softness”) of a protein structure and relate it to biological function and …

Notable recent developments in the use of normal mode methods to study protein dynamics
include the use of quasiharmonic descriptions in crystallographic and NMR refinement …

The two-volume Encyclopedia of Supramolecular Chemistry offers authoritative, centralized
information on a rapidly expanding interdisciplinary field. User-friendly and high-quality …

The use of molecular dynamics simulation to investigate the properties of hydration water
around proteins is outlined. A variety of structural and dynamical properties of the protein …

Multicolour near-infrared femtosecond experiments of a genetically modified bacterial
reaction centre show that the phase of two excited-state vibrational modes is conserved for a …

Various types of large-amplitude molecular deformation are ubiquitously involved in the
functions of biological macromolecules, especially supramolecular complexes. They can be …

Freeze-Drying/Lyophilization Of Pharmaceutical & Biological Products, Revised and Expanded
Page 1 DRUGS AND THE PHARMACEUTICAL SCIENCES Executive Editor James Swarbrick …

The dynamics of proteins in solution includes a variety of processes, such as backbone and
side-chain fluctuations, interdomain motions, as well as global rotational and translational …

The aim of the book is to introduce the reader to the kinetic analysis of a wide range of
biological processes at the molecular level. It is intended to show that the same approach …

▪ Abstract Although protein function is thought to depend on flexibility, precisely how the
dynamics of the molecule and its environment contribute to catalytic mechanisms is unclear …