Analytical Approach to the Protein Design Problem
- 22 November 1999
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 83 (21), 4437-4440
- https://doi.org/10.1103/physrevlett.83.4437
Abstract
We present an analytical method for determining the designability of protein structures. We apply our method to the case of two-dimensional lattice structures, and give a systematic solution for the spectrum of any structure. Using this spectrum, the designability of a structure can be estimated. We outline a hierarchy of structures, from most to least designable, and show that this hierarchy depends on the potential that is used.Keywords
This publication has 14 references indexed in Scilit:
- Effect of alphabet size and foldability requirements on protein structure designabilityProteins-Structure Function and Bioinformatics, 1999
- Highly designable protein structures and inter-monomer interactionsJournal of Physics A: General Physics, 1998
- Protein design: a perspective from simple tractable modelsFolding and Design, 1998
- De Novo Protein Design: Fully Automated Sequence SelectionScience, 1997
- Emergence of Preferred Structures in a Simple Model of Protein FoldingScience, 1996
- A new approach to the design of stable proteinsProtein Engineering, Design and Selection, 1993
- Engineering of stable and fast-folding sequences of model proteins.Proceedings of the National Academy of Sciences of the United States of America, 1993
- Implications of thermodynamics of protein folding for evolution of primary sequencesNature, 1990
- Spin glasses and the statistical mechanics of protein folding.Proceedings of the National Academy of Sciences of the United States of America, 1987
- Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximationMacromolecules, 1985