Folding behaviors of apocytochrome b 5 and its mutants: Insights from high temperature molecular dynamics simulations
Saved in:
| Title: | Folding behaviors of apocytochrome b |
|---|---|
| Authors: | Lin, Ying-Wu1,2 linlinying@hotmail.com, Nie, Chang-Ming1, Liao, Li-Fu1 |
| Source: | Journal of Molecular Structure: THEOCHEM. Sep2009, Vol. 910 Issue 1-3, p154-162. 9p. |
| Subjects: | Protein folding, Denaturation of proteins, Cytochrome b, Genetic mutation, High temperatures, Molecular dynamics, Hemoproteins, Carrier proteins |
| Abstract: | Abstract: Apocytochrome b 5 (apocyt b 5) with heme removal from the heme-binding core 1, and its mutants with amino acid replaced in the hydrophobic core 2, namely apocyt b 5 Y7P, P81A and H15R/S20E, have been subjected to molecular dynamics (MD) simulation at high temperature (500K) for elucidating their folding behaviors. The early events upon thermal induced unfolding were found to be in good agreement with available experimental results, and the lowest stability of Y7P was predicted among the four apoproteins. The influences of these key residues on protein folding behavior were compared directly at an atomic level. At the same time, the influences of non-native interactions of hydrogen bonds and salt-bridges on protein stabilities were analyzed in detail. The insights from current MD simulations are valuable for understanding the apoprotein folding and the holoprotein formation in terms of heme proteins. [Copyright &y& Elsevier] |
| Copyright of Journal of Molecular Structure: THEOCHEM is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
Be the first to leave a comment!
