Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

Theoretical and experimental studies have firmly established that protein folding can be
described by a funneled energy landscape. This funneled energy landscape is the result of …

Refolding intermediates of proteins, including molten globules, are likely to undergo
dynamic conformational transitions. In this work, thermal unfolding and refolding of bovine β …

Ribonuclease HII from hyperthermophile Thermococcus kodakaraensis (Tk-RNase HII) is a
kinetically robust monomeric protein. The conformational stability and folding kinetics of Tk …

Although the folding rates of proteins have been studied extensively, both experimentally
and theoretically, and many native state topological parameters have been proposed to …

The actin filament network is in part remodeled by the action of a family of filament severing
proteins that are responsible for modulating the ratio between monomeric and filamentous …

The three‐dimensional structure of the enzyme 3‐isopropylmalate dehydrogenase from the
bacterium T hermus thermophilus in complex with Mn2+, its substrate isopropylmalate and …

Examining the chemical modification of biological polymers and the emerging applications
of this technology, Chemical Modification of Biological Polymers reflects the change in …

The domain closure associated with the catalytic cycle is described at an atomic level, based
on pairwise comparison of the X-ray structures of homodimeric Thermus thermophilus …

Enzyme function depends on specific conformational motions. We show that the temperature
dependence of enzyme kinetic parameters can provide insight into these functionally …