| Range |
Table - link
|
| Organism |
Generic |
| Reference |
Lobanov MIu, Bogatyreva NS, Galzitskaia OV. Radius of gyration as an indicator
of protein structure compactness. Mol Biol (Mosk). 2008 Jul-Aug42(4):701-6. p.625 (p.3 of 6) table 1PubMed ID18856071
|
| Method |
Abstract:"Statistical analysis of radii of gyration for 3769 protein structures from four general structural classes (all-alpha, all-beta, alpha/beta, alpha + beta) demonstrates that each class of proteins has its own class-specific radius of gyration, which determines compactness of protein structures: alpha-proteins have the largest radius of gyration." For protein classes see heading "Classes" in link |
| Comments |
p.624 (p.2 of 6) left column bottom paragraph:” [Investigators] have previously examined the four major protein classes (a, ß, a/ß, and a+ß) and have revealed a difference in the contact number per residue [refs 27, 28]. An optimal ratio between the mean conformational entropy and mean energy of the interaction between residues has been determined for rapid protein folding [ref 27].” p.625 (p.3 of 6) right column bottom paragraph:"[Investigators] have earlier found that the mean contact number per residue differs among the four major classes of proteins. In this work, [investigators] computed the radius of gyration of a protein molecule from its spatial structure, taking atoms as balls of the same radius 1.5 Å and the same mass. The radius of gyration was computed for a preset size range, with the average protein size being approximately the same in each structural class (Table 1). Each structural class of proteins had its own class-specific radius of gyration (Table 1, Fig. 1)." Note-there is a discrepancy between page numbers, probably due to difference between the original and the translation |
| Entered by |
Uri M |
| ID |
111732 |