NMR study and molecular dynamics simulations of optimized beta-hairpin fragments of protein G
| Autor: | Beatrice M. P. Huyghues-Despointes, J. Martin Scholtz, Yun Wei, Jerry Tsai |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Molecular Sequence Data Peptide Nerve Tissue Proteins Crystallography X-Ray Biochemistry Protein Structure Secondary Turn (biochemistry) Molecular dynamics Residue (chemistry) Structural Biology Computer Simulation Amino Acid Sequence Molecular Biology Peptide sequence Nuclear Magnetic Resonance Biomolecular chemistry.chemical_classification biology Nuclear magnetic resonance spectroscopy Peptide Fragments Protein Structure Tertiary Folding (chemistry) Crystallography chemistry Amino Acid Substitution biology.protein Biophysics Thermodynamics Protein G |
| Zdroj: | Proteins. 69(2) |
| ISSN: | 1097-0134 |
| Popis: | The stability and structure of several beta-hairpin peptide variants derived from the C-terminus of the B1 domain of protein G were investigated by a number of experimental and computational techniques. Our analysis shows that the structure and stability of this hairpin can be greatly affected by one or a few simple mutations. For example, removing an unfavorable charge near the N-terminus of the peptide (Glu42 to Gln or Thr) or optimization of the N-terminal charge-charge interactions (Gly41 to Lys) both stabilize the peptide, even in water. Furthermore, a simple replacement of a charged residue in the turn (Asp47 to Ala) changes the beta-turn conformation. Finally, we show that the effects of combining these single mutations are additive, suggesting that independent stabilizing interactions can be isolated and evaluated in a simple model system. Our results indicate that the structure and stability of this beta-hairpin peptide can be modulated in numerous ways and thus contributes toward a more complete understanding of this important model beta-hairpin as well as to the folding and stability of larger peptides and proteins. |
| Databáze: | OpenAIRE |
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