Probing the conformational state of a truncated staphylococcal nuclease r using time of flight mass spectrometry with limited proteolysis

European Journal of Biochemistry

Volumn 268, Issue 15, 2001, Pages 4227-4232

  Yang, Feng ^a   Cheng, Yuan ^a   Peng, Jiarou ^b   Zhou, Junmei ^a   Jing, Guozhong ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

Author keywords

Conformation; Ligand binding; Mass spectrometry; Truncated staphylococcal nuclease

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; ENDOPROTEINASE GLU C; ENZYME SNR135; LIGAND; NUCLEASE; PROTEINASE; STAPHYLOCOCCAL NUCLEASE R; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ELECTROPHORESIS; ENZYME ACTIVE SITE; ENZYME STABILITY; HYDROLYSIS; LIGAND BINDING; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION;

BINDING SITES; HYDROLYSIS; LIGANDS; MASS SPECTROMETRY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SERINE ENDOPEPTIDASES; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STAPHYLOCOCCUS; TIME FACTORS;

EID: 0034819326     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02337.x     Document Type: Article

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