A Unified Model of $α$-Helix/$β$-Sheet/Random-Coil Transition in Proteins
| dc.creator | Hong, Liu | |
| dc.creator | Lei, JinZhi | |
| dc.date | 2007-11-06 | |
| dc.date.accessioned | 2026-06-02T21:43:13Z | |
| dc.description | The theory of transition between $α$-helix, $β$-sheet and random coil conformation of a protein is discussed through a simple model, that includes both short and long-range interactions. Besides the bonding parameter and helical initiation factor in Zimm-Bragg model, three new parameters are introduced to describe beta structure: the local constraint factor for a single residue to be contained in a $β$-strand, the long-range bonding parameter that accounts for the interaction between a pair of bonded $β$-strands, and a correction factor for the initiation of a $β$-sheet. Either increasing local constraint factor or long-range bonding parameter can cause a transition from $α$-helix or random coil conformation to $β$-sheet conformation. The sharpness of transition depends on the competition between short and long-range interactions. Other effective factors, such as the chain length and temperature, are also discussed. In this model, the entropy due to different ways to group $β$-strands into different $β$-sheets gives rise to significant contribution to partition function, and makes major differences between beta structure and helical structure. | |
| dc.description | 8 pages, 7 figures | |
| dc.identifier | https://arxiv.org/abs/0711.0846 | |
| dc.identifier | http://arxiv.org/abs/0711.0846 | |
| dc.identifier.uri | https://demo.dspace.org/handle/10673/1989 | |
| dc.subject | Biological Physics | |
| dc.subject | Soft Condensed Matter | |
| dc.subject | Biomolecules | |
| dc.title | A Unified Model of $α$-Helix/$β$-Sheet/Random-Coil Transition in Proteins | |
| dc.type | text |