The role of fluctuations in protein thermostability has recently received considerable
attention. In the current literature a dualistic picture can be found: thermostability seems to …

An understanding of the forces that contribute to stability is pivotal in solving the protein‐
folding problem. Classical theory suggests that disulfide bonds stabilize proteins by …

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 …

Several sequence and structural factors have been proposed to contribute toward greater
stability of thermophilic proteins. Here we present a statistical examination of structural and …

A non-redundant set of 1154 protein structures from the Protein Data Bank was examined
with respect to close interactions between CH-donor and π-acceptor groups. A total of …

Background: Proteins from thermophilic organisms usually show high intrinsic thermal
stability but have structures that are very similar to their mesophilic homologues. From …

Recent years have witnessed an explosion of sequence and structural information for
proteins from hyperthermophilic and thermophilic organisms. Complete genome sequences …

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 …

Protein–protein recognition plays an essential role in structure and function. Specific non-
covalent interactions stabilize the structure of macromolecular assemblies, exemplified in …

Thermozymes are enzymes that evolved in thermophiles (organisms thriving at 60-8O'C)
and hyperthermophiles(organisms thriving at 280%). Whereas thermophiles are classed as …