Folding of the twisted .beta.-sheet in bovine pancreatic trypsin inhibitor

The dominant role of local interactions has been demonstrated for the formation of the strongly twisted antiparallel beta-sheet structure consisting of residues 18-35 in bovine pancreatic trypsin inhibitor. Conformational energy minimization has indicated that this beta-sheet has a strong twist even...

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Veröffentlicht in:	Biochemistry (Easton) 1985-12, Vol.24 (27), p.7948-7953
Hauptverfasser:	Chou, Kuo Chen, Nemethy, George, Pottle, Marcia S, Scheraga, Harold A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Biological and medical sciences Cattle Fundamental and applied biological sciences. Psychology Macromolecular Substances Models, Molecular Molecular biophysics Protein Conformation Structure in molecular biology Tridimensional structure Trypsin Inhibitor, Kazal Pancreatic Trypsin Inhibitors
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