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 activity. …

It is now clear that the understanding of halophilic adaptation at a molecular level requires a
strategy of complementary experiments, combining molecular biology, biochemistry, and …

… Hydration values of approximately 044 g of water per g of protein (h=044 g/g) correspond to
… experiments have a maximum hydration of hy045 g/g. Protein powder dynamics has been …

The structure of the protein–solvent interface is the subject of controversy in theoretical
studies and requires direct experimental characterization. Three proteins with known atomic …

NEUTRON diffraction combined with the use of selectively deuterated lipids can provide
detailed information on the molecular structure of membranes. Because of the large difference …

… sample (0.55 g of2H20 per g of BR) and a moderately dry sample (0.02 g of 2H20 per g of
BR, in … by 2H20 in two successive centrifugation steps (100,000 x g, 100C, 1 hr) ofthe isolated …

Neutron diffraction experiments on selectively deuterated lipids provide a new method of
determining to a segmental resolution the mean conformation of a lipid molecule as projected …

… If C is in g 1-1 and St is in cm3, we must write … The experiments are done in 1-mm quartz
cells with concentrations close to 5 g 1-1. This corresponds to a uv transmission of about 0.5, so …

Acetylcholinesterase (AChE) terminates nerve‐impulse transmission at cholinergic synapses
by rapid hydrolysis of the neurotransmitter, acetylcholine. Substrate traffic in AChE involves …

… Jacrot & Zaccai' (18) have discussed this application of neutron scattering to biological
molecules. In H20 solution, because of the small negative value of pO, the density increment for …