Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability.

By Marc Robinson-Rechavi, Adam Godzik. 2005

59 citations recorded by the source corpus.

Despite numerous studies, understanding the structural basis of protein stability in thermophilic organisms has remained elusive. One of the main reasons is the limited number of thermostable protein structures available for analysis, but also the difficulty in identifying relevant features to compare. Notably, an intuitive feeling of "compactness" of thermostable proteins has eluded quantification. With the unprecedented opportunity to assemble a data set for comparative analyses due to the recent advances in structural genomics, we can now revisit this issue and focus on experimentally determined structures of proteins from the hyperthermophilic bacterium Thermotoga maritima. We find that 73% of T. maritima proteins have higher contact order than their mesophilic homologs. Thus, contact order, a structural feature that was originally introduced to explain differences in folding rates of different protein families, is a significant parameter that can now be correlated with thermostability.

Subfields: Materials Chemistry, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

In Molecular Biology

Citations in the corpus

Toward the estimation of the absolute quality of individual protein structure models (2010, methodology): “The dataset of pairs of homologous proteins as described in RobinsonRechavi and Godzik (Robinson-Rechavi and Godzik, 2005) has been used.”