Open AccessA Study of the Lysyl Residues in the Basic Pancreatic Trypsin Inhibitor using 1 H Nuclear Magnetic Resonance at 360 MHz
Author(s) -
BROWN Larry R.,
MARCO Antonio,
WAGNER Gerhard,
WÜTHRICH Kurt
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb10102.x
Subject(s) - intermolecular force , tyrosine , crystallography , trypsin , intramolecular force , chemistry , resonance (particle physics) , lysine , nuclear magnetic resonance , molecule , stereochemistry , biochemistry , amino acid , physics , organic chemistry , enzyme , particle physics
Fourier transform 1 H nuclear magnetic resonance (NMR) experiments at 360 MHz using convolution difference techniques to improve the spectral resolution were employed to investigate the resonances of the lysyl residues in bovine pancreatic trypsin inhibitor. The observations in both native protein and in chemically modified protein containing N e ‐dimethyllysine show that three of the four lysines extend predominantly freely into the solvent, whereas lysine‐41 is involved in an intramolecular interaction with tyrosine‐10. Since in the single crystal structure tyrosine‐10 is involved in an intermolecular interaction with arginine‐42 of the neighboring protein molecule, the NMR data thus reveal a local conformation difference for bovine pancreatic trypsin inhibitor in solution and in the crystalline form which appears to result primarily from intermolecular interaction in the crystal lattice.