Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200°C
AUTOR(ES)
Hiller, Reuben
FONTE
The National Academy of Sciences of the USA
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23458Documentos Relacionados
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