Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles.

ABSTRACT:

Background

The database of protein structures contains representatives from organisms with a range of growth temperatures. Various properties have been studied in a search for the molecular basis of protein adaptation to higher growth temperature. Charged groups have emerged as key distinguishing factors for proteins from thermophiles and mesophiles.

Results

A dataset of 291 thermophile-derived protein structures is compared with mesophile proteins. Calculations of electrostatic interactions support the importance of charges, but indicate that increases in charge contribution to folded state stabilisation do not generally correlate with the numbers of charged groups. Relative propensities of charged groups vary, such as the substitution of glutamic for aspartic acid sidechai

SUBMITTER: Greaves RB 

PROVIDER: S-EPMC1851960 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature