Why are some proteins structures so common?
- 16 April 1996
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (8) , 3341-3345
- https://doi.org/10.1073/pnas.93.8.3341
Abstract
Many biological proteins are observed to fold into one of a limited number of structural motifs. By considering the requirements imposed on proteins by their need to fold rapidly, and the ease with which such requirements can be fulfilled as a function of the native structure, we can explain why certain structures are repeatedly observed among proteins with negligible sequence similarity. This work has implications for the understanding of protein sequence structure relationships as well as protein evolution.Keywords
This publication has 27 references indexed in Scilit:
- Impact of Local and Non-local Interactions on Thermodynamics and Kinetics of Protein FoldingJournal of Molecular Biology, 1995
- Phosphorescence Reveals a Continued Slow Annealing of the Protein Core following Reactivation of Escherichia coli Alkaline PhosphataseBiochemistry, 1995
- Protein superfamilles and domain superfoldsNature, 1994
- How does a protein fold?Nature, 1994
- From sequences to shapes and back: a case study in RNA secondary structuresProceedings Of The Royal Society B-Biological Sciences, 1994
- Kinetics of Protein Folding: A Lattice Model Study of the Requirements for Folding to the Native StateJournal of Molecular Biology, 1994
- Why are the same protein folds used to perform different functions?FEBS Letters, 1993
- The Energy Landscapes and Motions of ProteinsScience, 1991
- Why do globular proteins fit the limited set of foldin patterns?Progress in Biophysics and Molecular Biology, 1987
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973