Article
Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two-dimensional nuclear magnetic resonance.
Protein science : a publication of the Protein Society - 1 Jan 1992
Hurle M R, Eads C D, Pearlman D A, Seibel G L, Thomason J, Kosen P A, Kollman P, Anderson S, Kuntz I D
Abstract excerpt
Structural perturbations due to a series of mutations at the 30-51 disulfide bond of bovine pancreatic trypsin inhibitor have been explored using NMR. The mutants replaced cysteines at positions 30 and 51 by alanine at position 51 and alanine, threonine, or valine at position 30. Chemical shift changes occur in residues proximate to the site of mutation. NOE assignments were made using an automated procedure,...
Topics
- Amino Acid Sequence
- Animals
- Aprotinin
- Cattle
- Cysteine
- Disulfides
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Protein Structure, Tertiary