Article
A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins.
Proceedings of the National Academy of Sciences of the United States of America - 19 Mar 2002
Zhou Huan-Xiang
Abstract excerpt
Characterization of the unfolded state is essential for understanding the protein folding problem. In the unfolded state, a protein molecule samples vastly different conformations. Here I present a simple theoretical method for treating residual charge-charge interactions in the unfolded state. The method is based on modeling an unfolded protein as a Gaussian chain. After sampling over all conformations, the...
Topics
- Bacterial Proteins
- Bacteriophage T4
- Hydrogen-Ion Concentration
- Isoenzymes
- Models, Chemical
- Muramidase
- Mutation
- Myoglobin
- Normal Distribution
- Protein Denaturation
- Protein Folding
- Proteins
- Ribonuclease T1
- Ribonuclease, Pancreatic
- Ribonucleases
- Static Electricity
- Thermodynamics