Article
Paired natural cysteine mutation mapping: aid to constraining models of protein tertiary structure.
Protein science : a publication of the Protein Society - 1 Nov 1995
Kreisberg R, Buchner V, Arad D
Abstract excerpt
This paper discusses the benefit of mapping paired cysteine mutation patterns as a guide to identifying the positions of protein disulfide bonds. This information can facilitate the computer modeling of protein tertiary structure. First, a simple, paired natural-cysteine-mutation map is presented...
Topics
- Algorithms
- Amino Acid Sequence
- Animals
- Computer Simulation
- Conserved Sequence
- Cysteine
- Disulfides
- Endopeptidases
- Humans
- Models, Molecular
- Mutation
- Protein Folding
- Protein Structure, Tertiary
- Sequence Alignment