Perfect temperature for protein structure prediction and folding
- 1 October 1995
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 23 (2) , 151-162
- https://doi.org/10.1002/prot.340230205
Abstract
We have investigated the influence of the “noise” of inevitable errors in energetic parameters on-protein structure prediction. Because of this noise, only a part of all the interactions operating in a protein chain can be taken into account, and therefore a search for the energy minimum becomes inadequate for protein structure prediction. One can rather rely on statistical mechanics: a calculation carried out at a temperature T* somewhat below that of protein melting gives the best possible, though always approximate prediction. The early stages of protein folding also “take into account” only a part of all the interactions; consequently, the same temperature T* is favorable for the self-organization of native-like intermediates in protein folding.Keywords
This publication has 31 references indexed in Scilit:
- When is a potential accurate enough for structure prediction? Theory and application to a random heteropolymer model of protein foldingThe Journal of Chemical Physics, 1994
- Why are the same protein folds used to perform different functions?FEBS Letters, 1993
- The folding of an enzyme: IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedureJournal of Molecular Biology, 1992
- Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfoldingJournal of Molecular Biology, 1992
- Prediction of progress at lastNature, 1991
- How does protein synthesis give rise to the 3D‐structure?FEBS Letters, 1991
- Implications of thermodynamics of protein folding for evolution of primary sequencesNature, 1990
- Why do globular proteins fit the limited set of foldin patterns?Progress in Biophysics and Molecular Biology, 1987
- Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroismFEBS Letters, 1987
- A theory of protein molecule self-organizationJournal of Molecular Biology, 1976