Sidechain torsional potentials and motion of amino acids in porteins: bovine pancreatic trypsin inhibitor

摘要: Abstract Conformational potentials of sidechains in the bovine pancreatic trypsin inhibitor have been studied with an empirical energy function. Calculated minimumenergy positions are excellent agreement x-ray structure for core or at surface protein; as expected, angles that directed out into solvent do not agree calculated values. The contributions to analyzed and compared free amino acid. Although there is a large restriction available conformational space due nonbonded interactions, minimum protein close those acid; significance this result discussed. To estimate effective barriers rotation aromatic rings (tyrosine phenylalanine), calculations done which permitted relax function ring orientation. Thr resulting barriers, much lowere than rigid used evaluate rates; comparison made nuclear magnetic resonance data.