PMID: 2474Feb 2, 1976

A study of the lysyl residues in the basic pancreatic trypsin inhibitor using 1H nuclear magnetic resonance at 360 Mhz

European Journal of Biochemistry
L R BrownK Wüthrich


Fourier transform 1H 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 Nepsilon-dimethyllsysine 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.


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Feb 1, 1997·Protein Science : a Publication of the Protein Society·S T WlodekJ A McCammon
Feb 15, 1979·Nature·M Karplus, J A McCammon
Jun 15, 1977·European Journal of Biochemistry·J H Bradbury, L R Brown
Nov 21, 2015·Bioconjugate Chemistry·Sacha Thierry LardaRobert Scott Prosser
Jul 29, 2004·Proteins·Michael S LeeCharles L Brooks
Jan 1, 1985·CRC Critical Reviews in Biochemistry·J B MatthewS J Shire
Nov 21, 2009·Protein Engineering, Design & Selection : PEDS·Ri-Bo HuangKuo-Chen Chou
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Oct 1, 1985·International Journal of Peptide and Protein Research·J P Laussac, B Sarkar
Jun 18, 1996·Biochemistry·J AntosiewiczM K Gilson

Related Concepts

Hydrogen-Ion Concentration
Lysine Hydrochloride
In Vivo NMR Spectroscopy
Protein Conformation
Pancreatic Trypsin Secretory Inhibitor, Kazal
Trypsin Inhibitors

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