On a general definition of the set of native conformations for globular polypeptides
Morehouse School of Medicine, Morehouse School of Medicine, Atlanta, Georgia, United States of America
- Published
- Accepted
- Subject Areas
- Biochemistry, Bioengineering, Biophysics, Biotechnology, Molecular Biology
- Keywords
- Globular peptides, Protein activity, Native conformation, Allosteric modulation
- Copyright
- © 2016 Jeff-Eke
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
- Cite this article
- 2016. On a general definition of the set of native conformations for globular polypeptides. PeerJ PrePrints 4:e1735v1 https://doi.org/10.7287/peerj.preprints.1735v1
Abstract
Here we question the generality of the conventional definition of a native conformation –as the 3-dimensional conformation of an entire globular polypeptide molecule. Although considered common knowledge, and thus not explicitly stated in modern writings, this definition of native conformations has a history as old as the protein folding problem. We attempt a more applicable definition that better correlates with functional activity and thus may be a more suitable substitute for the current convention.
Author Comment
We question the generality of the conventional definition of a native conformation and attempt a more applicable definition.