Free energy calculations show that acidic P1 variants undergo large pK a shifts upon binding to trypsin

Proteins: Structure, Function and Genetics

Volumn 64, Issue 3, 2006, Pages 740-748

  Brandsdal, Bjørn O ^a   Smalås, Arne O ^a   Åqvist, Johan ^b  

^a UNIVERSITY OF TROMSØ   (Norway)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

Free energy perturbation; Linear interaction energy method; Linear response; Molecular dynamics simulations; Protein protein interactions; Serine proteinases

Indexed keywords

GLUTAMIC ACID; PROTEINASE INHIBITOR; SERINE PROTEINASE; TRYPSIN;

AMINO ACID COMPOSITION; ARTICLE; BINDING SITE; ENZYME INHIBITOR INTERACTION; ENZYME MECHANISM; ENZYME SPECIFICITY; LINEAR ENERGY TRANSFER; PH; PKA; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEINASE INHIBITION; PROTON TRANSPORT; X RAY CRYSTALLOGRAPHY;

APROTININ; ASPARTIC ACID; BINDING SITES; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ENTROPY; GLUTAMIC ACID; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SERINE ENDOPEPTIDASES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THERMODYNAMICS; TRYPSIN; TRYPSIN INHIBITORS;

EID: 33746268441     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20940     Document Type: Article

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