Structural comparison between wild-type and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the α-helix conformation ?

Journal of Structural and Functional Genomics

Volumn 1, Issue 1, 2000, Pages 26-42

  Shimba, Nobuhisa ^a   Kariya, Eri ^a   Tate, Shin Ichi ^a   Kaji, Hiroyuki ^a   Kainosho, Masatsune ^a  

^a TOKYO METROPOLITAN UNIVERSITY   (Japan)

Author keywords

NMR structure; P25S cystatin A; Wild type cystatin A; helix deformation

Indexed keywords

CYSTATIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; GENETICS; HUMAN; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CYSTATINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 0009762926     PISSN: 1345711X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1011380315619     Document Type: Review

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