Different molecular size scaling regimes for inner and outer regions of proteins
- 1 September 1996
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 54 (3) , 3044-3047
- https://doi.org/10.1103/physreve.54.3044
Abstract
We study the rough statistical features of size scaling in protein backbones by using molecular descriptors associated with their central and external regions. By using a diverse set of experimental structures, we show that the mean radius of gyration and the span of backbones scale differently, leading to a ratio of ‘‘inner’’ and ‘‘outer’’ scaling size exponents of /≊0.8. The span of average proteins is found to scale with the number of amino acids as R∼, with 1/21996 The American Physical Society.
Keywords
This publication has 18 references indexed in Scilit:
- Fast Monte Carlo algorithms for knotted polymersPhysical Review E, 1995
- Scaling regimes of molecular size and self-entanglements in very compact proteinsPhysical Review E, 1995
- Random hydrophilic-hydrophobic copolymersJournal de Physique II, 1994
- Global Statistics of Protein Sequences: Implications for the Origin, Evolution, and Prediction of StructureAnnual Review of Biophysics, 1994
- Scaling behavior of some molecular shape descriptors of polymer chains and protein backbonesPhysical Review E, 1994
- Protein structure and polymer collapseThe Journal of Chemical Physics, 1993
- Polymer Principles in Protein Structure and StabilityAnnual Review of Biophysics, 1991
- Theory for the folding and stability of globular proteinsBiochemistry, 1985
- Critical exponents from field theoryPhysical Review B, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977