Molecular dynamics simulations were performed to unfold a homologous pair of thermophilic and mesophilic cold shock proteins at high temperatures. The two proteins differ in just 11 of 66 residues and have very similar structures with a closed five-stranded antiparallel beta-barrel. A long flexible loop connects the N-terminal side of the barrel, formed by three strands (beta1-beta3), with the ...

Structural analysis is useful in elucidating structural features responsible for enhanced thermal stability of proteins. However, due to the rapid increase of sequenced genomic data, there are far more protein sequences than the corresponding three-dimensional (3D) structures. The usual sequence-based amino acid composition analysis provides useful but simplified clues about the amino acid type...

Anoxybacillus suryakundensis strain JS1(T), a facultative anaerobic, moderately thermophilic, alkalitolerant bacterium, was isolated from a hot spring. The estimated genome is 2.6 Mb and encodes 2,668 proteins.

Environmental temperature plays an important role in the cell life [1]. There are four classes of organism in relation to their optimal growth temperature namely hyperthermophile (>80◦C), thermophile (45-80◦C), mesophile (20-45◦C) and psychrophile (<20◦C) [2]. Thermal stability is defined as the ability of material to resist changes in physical structure or chemical irreversibility, or spatial ...

A comparative study of amino acid sequence and physicochemical properties indicates the affiliation of protein from the nitrilase/cyanide hydratase family. This family contains nitrilases that break carbon-nitrogen bonds and appear to be involved in the reduction of organic nitrogen compounds and ammonia production. They all have distinct substrate specificity and include nitrilase, cyanide hyd...

Temperature, perhaps more than any other environmental factor, is likely to influence the evolution of all organisms. It is also a very interesting factor to understand how genomes are shaped by selection over evolutionary timescales, as it potentially affects the whole genome. Among thermophilic prokaryotes, temperature affects both codon usage and protein composition to increase the stability...

C-Phycocyanins from two thermophilic strains of Synechococcus lividus that grow within different temperature ranges have been shown to be unalike. The aggregation ability of these two C-phycocyanins in sedimentation-velocity experiments varied dramatically. Surprisingly, the aggregation properties of mesophilic C-phycocyanins were found to lie between those of the two thermophilic proteins. Und...

Asymmetrical patterns of amino acid substitution in proteins of organisms living at moderate and high temperatures (mesophiles and thermophiles, respectively) are generally taken to indicate selection favoring different amino acids at different temperatures due to their biochemical properties. If that were the case, comparisons of different pairs of mesophilic and thermophilic taxa would exhibi...