Article
Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins.
Biochemistry - 13 Apr 1993
Otting G, Liepinsh E, Wüthrich K
Abstract excerpt
Two conformational isomers were observed in the 1H nuclear magnetic resonance (NMR) spectra of the basic pancreatic trypsin inhibitor (BPTI) and of a mutant protein with Gly 36 replaced by Ser, BPTI(G36S). The less abundant isomer differs from the major conformation by different chirality of the Cys 14-Cys 38 disulfide bond. In BPTI, the population of the minor conformer increases from about 1.5% at 4 degrees C...
Topics
- Amino Acid Sequence
- Aprotinin
- Crystallization
- Disulfides
- Glycine
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Recombinant Proteins
- Thermodynamics