Flexibility of $α$-helices: Results of a statistical analysis of database protein structures
| dc.creator | Emberly, Eldon G. | |
| dc.creator | Mukhopadhyay, Ranjan | |
| dc.creator | Wingreen, Ned S. | |
| dc.creator | Tang, Chao | |
| dc.date | 2002-09-25 | |
| dc.date.accessioned | 2026-07-07T02:47:26Z | |
| dc.date.available | 2026-07-07T02:47:26Z | |
| dc.description | $α$-helices stand out as common and relatively invariant secondary structural elements of proteins. However, $α$-helices are not rigid bodies and their deformations can be significant in protein function ({\it e.g.} coiled coils). To quantify the flexibility of $α$-helices we have performed a structural principal-component analysis of helices of different lengths from a representative set of protein folds in the Protein Data Bank. We find three dominant modes of flexibility: two degenerate bend modes and one twist mode. The data are consistent with independent Gaussian distributions for each mode. The mode eigenvalues, which measure flexibility, follow simple scaling forms as a function of helix length. The dominant bend and twist modes and their harmonics are reproduced by a simple spring model, which incorporates hydrogen-bonding and excluded volume. As an application, we examine the amount of bend and twist in helices making up several coiled-coil proteins. Incorporation of $α$-helix flexibility into structure refinement and design is discussed. | |
| dc.description | 13 pages, 6 figures | |
| dc.identifier | https://arxiv.org/abs/cond-mat/0209595 | |
| dc.identifier | http://arxiv.org/abs/cond-mat/0209595 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/20010 | |
| dc.subject | Statistical Mechanics | |
| dc.subject | Soft Condensed Matter | |
| dc.subject | Biomolecules | |
| dc.title | Flexibility of $α$-helices: Results of a statistical analysis of database protein structures | |
| dc.type | text |