Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation.
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Comparison of Two ESI MS Based H/D Exchange Methods for Extracting Protein Folding Energies.Structural systems biology evaluation of metabolic thermotolerance in Escherichia coliOn the physics of thermal-stability changes upon mutations of a protein.The fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model.The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model.Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range.
P2860
Thermal denaturations of staphylococcal nuclease wild-type and mutants monitored by fluorescence and circular dichroism are similar: lack of evidence for other than a two state thermal denaturation.
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2006年の論文
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Thermal denaturations of staph ...... wo state thermal denaturation.
@en
Thermal denaturations of staph ...... wo state thermal denaturation.
@nl
type
label
Thermal denaturations of staph ...... wo state thermal denaturation.
@en
Thermal denaturations of staph ...... wo state thermal denaturation.
@nl
prefLabel
Thermal denaturations of staph ...... wo state thermal denaturation.
@en
Thermal denaturations of staph ...... wo state thermal denaturation.
@nl
P2860
P1476
Thermal denaturations of staph ...... wo state thermal denaturation.
@en
P2093
Michael P Byrne
Wesley E Stites
P2860
P304
P356
10.1016/J.BPC.2006.10.014
P577
2006-11-28T00:00:00Z