Article
A molecular dynamics study of a model built Pro-36-Gly mutant derived from the potato carboxypeptidase A inhibitor protein.
Biochemical and biophysical research communications - 30 Apr 1991
Oliva B, Nilsson O, Wästlund M, Cardenas R, Querol E, Avilés F X, Tapia O
Abstract excerpt
A 120ps molecular dynamics (MD) trajectory was calculated and analyzed for a putative Pro-36-Gly mutant of the potato carboxypeptidase A (CPA) protein inhibitor (PCIm). The mutant protein's fold shows a large degree of stability, judged from its low alpha-carbon r.m.s. deviation from the X-ray structure of the wild type PCI (PCIw). The N-terminal tail of PCIm differs slightly less from the X-ray structure than it...
Topics
- Carboxypeptidases
- Carboxypeptidases A
- Models, Molecular
- Mutation
- Plant Proteins
- Protease Inhibitors
- Protein Conformation
- X-Ray Diffraction