Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry

Protein Science

Volumn 5, Issue 7, 1996, Pages 1282-1289

  Zhang, Zhongqi ^a,b   Smith, David L ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b FLORIDA STATE UNIVERSITY   (United States)

Author keywords

aldolase; amide hydrogen exchange; mass spectrometry; protein unfolding domains

Indexed keywords

AMIDE; DEUTERIUM; FRUCTOSE BISPHOSPHATE ALDOLASE; HYDROGEN; MUSCLE ENZYME;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STABILITY; EQUILIBRIUM CONSTANT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; RABBIT; TEMPERATURE DEPENDENCE; THERMAL EXPOSURE;

AMIDES; ANIMALS; FRUCTOSE-BISPHOSPHATE ALDOLASE; HYDROGEN; MASS SPECTROMETRY; MUSCLES; PROTEIN CONFORMATION; PROTEIN FOLDING; RABBITS;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0029897362     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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