Side-chain conformational entropy in protein unfolded states
โ Scribed by Trevor P. Creamer
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 138 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0887-3585
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
A model of nine proteins including side-chain atoms have been built from the known C a coordinates and amino acid sequences using a Monte Carlo Protein Building Annealing method. The Cartesian coordinates for the side-chain atoms were established with bond lengths and angles selected randomly from w
Contact surface area and chemical properties of atoms are used to concurrently predict conformations of multiple amino acid side chains on a fixed protein backbone. The combination of surface complementarity and solvent-accessible surface accounts for van der Waals forces and solvation free energy.
Although relatively rare, the tryptophan residue (Trp), with its large hydrophobic surface, has a unique role in the folded structure and the binding site of many proteins, and its fluorescence properties make it very useful in studying the structures and dynamics of protein molecules in solution. A