Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C.
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.
Hiller
R
R
The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA.
Zhou
Z H
ZH
Adams
M W
MW
Englander
S W
SW
D002942:Circular Dichroism; D004355:Drug Stability; D019791:Guanidine; D006358:Hot Temperature; D007700:Kinetics; D008961:Models, Structural; D011487:Protein Conformation; D011489:Protein Denaturation; D019711:Pyrococcus / Q000378:metabolism; D012416:Rubredoxins / Q000737:chemistry*; D013816:Thermodynamics
D012416:Rubredoxins; D019791:Guanidine