The nature of persistent interactions in two model β‐grasp proteins reveals the advantage of symmetry in stability
| Autor: | Jennifer L. Poutsma, Norou Diawara, Lesley H. Greene, John T. Bedford |
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| Rok vydání: | 2021 |
| Předmět: |
Protein Conformation
alpha-Helical Flexibility (anatomy) Archaeal Proteins Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences Stability (probability) Hydrophobic effect Molecular dynamics Bacterial Proteins 0103 physical sciences medicine Haloferax volcanii 010304 chemical physics biology Protein Stability Chemistry GRASP Streptococcus General Chemistry Symmetry (physics) 0104 chemical sciences Computational Mathematics medicine.anatomical_structure Structural stability biology.protein Biophysics Protein Conformation beta-Strand Protein G Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Journal of Computational Chemistry. 42:600-607 |
| ISSN: | 1096-987X 0192-8651 |
| Popis: | Two proteins within the β-grasp superfamily, the B1-domain of protein G and the small archaeal modifier protein 1, were investigated to elucidate the key determinants of structural stability at the level of individual interactions. These symmetrical proteins both contain two β-hairpins which form a sheet flanked by a central α-helix. They were subjected to high temperature molecular dynamics simulations and the detailed behavior of each long-range interaction was characterized. The results revealed that in GB1 the most stable region was the C-terminal hairpin and in SAMP1 it was the opposite, the N-terminal hairpin. Experimental results for GB1 support this finding. In conclusion, it appears that the difference in the location and number of hydrophobic interactions dictate the differential stability which is accommodated due to structural symmetry of the β-grasp fold. Thus, the hairpins are interchangeable and in nature this lends itself to adaptability and flexibility. |
| Databáze: | OpenAIRE |
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