Comparison of anionic and cationic trypsinogens: The anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure

Protein Science

Volumn 8, Issue 1, 1999, Pages 253-258

  Pasternak, Annette ^a   Ringe, Dagmar ^a   Hedstrom, Lizbeth ^a  

^a BRANDEIS UNIVERSITY   (United States)

Author keywords

Disorder order; Natively unfolded; Serine protease; X ray crystallography; Zymogen

Indexed keywords

ANION; APROTININ; ASPARTIC ACID; CATION; ISOLEUCINE; TRYPSIN; TRYPSINOGEN;

ARTICLE; AUTOLYSIS; CATTLE; CHEMICAL BOND; CIRCULAR DICHROISM; COMPARATIVE STUDY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; RAT;

EID: 0032952130     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.1.253     Document Type: Article

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