Revised Manuscript Received April 1, 1994* abstract: We survey all the known instances of
domain movements in proteins for which there is crystallographic evidence for …

Malate dehydrogenases (MDH, L-malate: NAD oxidoreductase, EC 1.1. 1.37), catalyze the
NAD/NADH-dependent interconversion of the substrates malate and oxaloacetate. This …

Comparative protein modeling is increasingly gaining interest since it is of great assistance
during the rational design of mutagenesis experiments. The availability of this method, and …

Methods developed originally to analyze domain motions from simulation [Proteins 27: 425–
437, 1997] are adapted and extended for the analysis of X‐ray conformers and for proteins …

An algorithm is presented for the accurate and rapid generation of multiple protein sequence
alignments from tertiary structure comparisons. A preliminary multiple sequence alignment is …

Protein-protein interaction sites in complexes of known structure are characterised using a
series of parameters to evaluate what differentiates them from other sites on the protein …

Orthologous proteins of species adapted to different temperatures exhibit differences in
stability and function that are interpreted to reflect adaptive variation in structural “flexibility.” …

Malate dehydrogenases are widely distributed and alignment of the amino acid sequences
show that the enzyme has diverged into 2 main phylogenetic groups. Multiple amino acid …

Sensitivity to temperature helps determine the success of organisms in all habitats, and is
caused by the susceptibility of biochemical processes, including enzyme function, to …

7α-Hydroxysteroid dehydrogenase (7α-HSDH; 1 EC 1.1. 1.159) is an NAD+-dependent
oxidoreductase belonging to the short-chain dehydrogenase/reductase (SDR) 1 family. It …