Probing the subtle conformational state of N138ND2-Q106O hydrogen bonding deletion mutant (Asn138Asp) of staphylococcal nuclease using time of flight mass spectrometry with limited proteolysis

Archives of Biochemistry and Biophysics

Volumn 434, Issue 1 SPEC. ISS., 2005, Pages 86-92

  Huang, Sun ^a   Zou, Xiajuan ^b   Guo, Peng ^a   Zhong, Lijun ^b   Peng, Jiarou ^b   Jing, Guozhong ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

Author keywords

Conformational integrity and stability; Ligand binding; Limited proteolysis; Mass spectrometry; Staphylococcal nuclease

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CALCIUM; GLUTAMINE; NUCLEASE; PROTEINASE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATION; DELETION MUTANT; HYDROGEN BOND; LIGAND BINDING; MASS SPECTROMETRY; MOLECULAR PROBE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TIME OF FLIGHT MASS SPECTROMETRY;

EID: 11144271355     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.abb.2004.10.011     Document Type: Article

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