Studies of the unfolding of an unstable mutant of staphylococcal nuclease: Evidence for low temperature unfolding and compactness of the high temperature unfolded state

Proteins: Structure, Function and Genetics

Volumn 28, Issue 2, 1997, Pages 227-240

  Eftink, Maurice R ^a   Ramsay, Glen D ^a,b   Beavers, Antonio ^a  

^a UNIVERSITY OF MISSISSIPPI   (United States)

^b Aviv Associates   (United States)

Author keywords

Circular dichroism; Cold unfolding; Fluorescence; Heat capacity change; Protein folding; Size exclusion chromatography

Indexed keywords

BACTERIAL ENZYME; MUTANT PROTEIN; NUCLEASE;

ANISOTROPY; ARTICLE; CIRCULAR DICHROISM; ENZYME DENATURATION; ENZYME STABILITY; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HIGH TEMPERATURE; HYDRODYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STAPHYLOCOCCUS;

CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; FLUORESCENCE POLARIZATION; MICROCOCCAL NUCLEASE; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS;

EID: 0030985878     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199706)28:2<227::AID-PROT11>3.0.CO;2-K     Document Type: Article

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