Abstract
The b-hairpin is a building block in the -sheet structure. Understanding the formation of the -hairpin may provide insight into the formation of -sheet structures in, for example, protein amyloids. In this study, we performed molecular dynamics (MD) simulations to investigate the temperature-dependent transition behaviors of the GB1 -hairpin peptide. The simulated results are analysed in terms of distances between pairs of peptide bonds and site-dependent dihedral angles. Our results show that the properties of the hairpin can be site-dependent and that the dependency is primarily associated with the hairpin's geometrical shape and specific interactions, such as hydrophobic clustering. Thus our study provides a foundation for the interpretation of probe-dependent experimental results.
Original language | English |
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Pages (from-to) | 915-928 |
Number of pages | 14 |
Journal | Journal of the Chinese Chemical Society |
Volume | 60 |
Issue number | 7 |
DOIs | |
State | Published - Jun 2013 |
Keywords
- Beta-hairpin; Protein folding; Site-dependent; Probe-dependent; MD simulations
- SIDE-CHAIN INTERACTIONS; STREPTOCOCCAL PROTEIN-G; MOLAR HEAT-CAPACITY; C-TERMINAL FRAGMENT; ENERGY LANDSCAPE; CIRCULAR-DICHROISM; AQUEOUS-SOLUTION; B1 DOMAIN; B3 DOMAIN; STABILITY