Molecular Dynamics Simulation of Ester-Linked Hen Egg White Lysozyme Reveals the Effect of Missing Backbone Hydrogen Bond Donors on the Protein Structure
✍ Scribed by Andreas P. Eichenberger; Zrinka Gattin; Garif Yalak; Wilfred F. van Gunsteren
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- German
- Weight
- 856 KB
- Volume
- 93
- Category
- Article
- ISSN
- 0018-019X
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✦ Synopsis
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 ester bonds. Molecular dynamics simulations of native and ester-linked lysozyme are compared with the native crystal structure and with NOE distance bounds derived from solution NMR experiments. The esterlinked protein shows a slight compaction while losing its native structure. However, it does not unfold completely. The structure remains compact due to its hydrophobic core and a changed network of hydrogen bonds involving side chains.