Consistent Picture of the Reversible Thermal Unfolding of Hen Egg-White Lysozyme from Experiment and Molecular Dynamics
✍ Scribed by Meersman, Filip; Atilgan, Canan; Miles, Andrew J.; Bader, Reto; Shang, Weifeng; Matagne, André; Wallace, B.A.; Koch, Michel H.J.
- Book ID
- 119207483
- Publisher
- Biophysical Society
- Year
- 2010
- Tongue
- English
- Weight
- 432 KB
- Volume
- 99
- Category
- Article
- ISSN
- 0006-3495
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Biomolecular force fields for use in molecular dynamics (MD) simulations of proteins, DNA, or membranes are generally parametrized against ab initio quantum-chemical and experimental data for small molecules. The application of a force field in a simulation of a biomolecular system, such as a protei
The three-dimensional structure of a protein is stabilized by a number of different atomic interactions. One of these is hydrogen bonding. Its influence on the spatial structure of the hen egg white lysozyme is investigated by replacing peptide bonds (except those of the two proline residues) by est