Work

Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200°C

Year: 1997

Type: article

Abstract: The rubredoxin protein from the hyperthermophilic archaebacterium Pyrococcus furiosus was examined by a hydrogen exchange method. Even though the protein does not exhibit reversible thermal unfolding, one can determine its stability parameters-free energy, enthalpy, entropy, and melting temperature-and also the distribution of stability throughout the protein, by using hydrogen exchange to measure the reversible cycling of the protein between native and unfolded states that occurs even under native conditions.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.94.21.11329

Authors: Reuben Hiller, Zhi H. Zhou, Michael W. W. Adams, S. Walter Englander

Institutions: University of Georgia, University of Pennsylvania

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases

Awards: METALLOPROTEIN STABILITY AND REDOX CHEMISTRY, G519003133, G5592925660, PROTEIN BONDING, STABILITY, AND FUNCTION