The bacterial cold shock proteins are small compact β-barrel proteins without disulfide
bonds, cis-proline residues or tightly bound cofactors. Bc-Csp, the cold shock protein from …

The cold shock proteins Bc-Csp from the thermophile Bacillus caldolyticus and Bs-CspB
from the mesophile Bacillus subtilis differ significantly in their conformational stability …

The cold shock protein Bc-Csp from the thermophile Bacillus caldolyticus differs from its
mesophilic homolog Bs-CspB from Bacillus subtilis by 15.8 kJ mol− 1 in the Gibbs free …

Residues Arg3 and Leu66 are crucially important for the enhanced stability of the cold shock
protein Bc-Csp from the thermophile Bacillus caldolyticus relative to its homologue Bs-CspB …

In previous work, we had identified stabilized forms of the cold-shock protein Bs-CspB from
Bacillus subtilis in a combinatorial library by an in vitro selection procedure. In this library …

The bacterial cold shock proteins (Csp) are widely used as models for the experimental and
computational analysis of protein stability. In a previous study, in vitro evolution was …

Bacillus subtilis possesses three homologous small cold shock proteins (CSPs; CspB,
CspC, CspD, sequence identity> 72%). They share a similar β-sheet structure, as shown by …

The thermophilic Bacillus caldolyticus cold shock protein (Bc-Csp) differs from the
mesophilic Bacillus subtilis cold shock protein B (Bs-CspB) in 11 of the 66 residues. Stability …

The two-state folding reaction of the cold shock protein from Bacillus caldolyticus (Bc-Csp) is
preceded by a rapid chain collapse. A fast shortening of intra-protein distances was …

Cold shock proteins (Csps) from mesophiles and thermophiles differ widely in their
stabilities, but show close structural similarity. Sequence variations involve mainly charged …