Structure-based thermodynamic design of peptide ligands: Application to peptide inhibitors of the aspartic protease endothiapepsin

Proteins: Structure, Function and Genetics

Volumn 30, Issue 1, 1998, Pages 74-85

  Luque, Irene ^a,b   Gómez, Javier ^a   Semo, Nora ^a   Freire, Ernesto ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b UNIVERSITY OF GRANADA   (Spain)

Author keywords

Folding and binding; Kinetics; Pepstatin A

Indexed keywords

ENDOTHIAPEPSIN; PEPSTATIN;

ACCURACY; ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; CALCULATION; DNA CONFORMATION; DNA STRUCTURE; DNA TEMPLATE; ENZYME ANALYSIS; ENZYME INHIBITION; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

ASPARTIC ENDOPEPTIDASES; ENZYME INHIBITORS; LIGANDS; MODELS, MOLECULAR; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 0031984455     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199801)30:1<74::AID-PROT7>3.0.CO;2-L     Document Type: Article

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