| Inter-residue interactions in protein folding and stability. | |
| | |
MedLine Citation:
|
PMID: 15288760 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
During the process of protein folding, the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form the stable native structure. The knowledge about inter-residue interactions in protein structures is very helpful to understand the mechanism of protein folding and stability. In this review, we introduce the classification of inter-residue interactions into short, medium and long range based on a simple geometric approach. The features of these interactions in different structural classes of globular and membrane proteins, and in various folds have been delineated. The development of contact potentials and the application of inter-residue contacts for predicting the structural class and secondary structures of globular proteins, solvent accessibility, fold recognition and ab initio tertiary structure prediction have been evaluated. Further, the relationship between inter-residue contacts and protein-folding rates has been highlighted. Moreover, the importance of inter-residue interactions in protein-folding kinetics and for understanding the stability of proteins has been discussed. In essence, the information gained from the studies on inter-residue interactions provides valuable insights for understanding protein folding and de novo protein design. |
| | |
Authors:
|
M Michael Gromiha; S Selvaraj |
Publication Detail:
|
Type: Journal Article; Review |
Journal Detail:
|
Title: Progress in biophysics and molecular biology Volume: 86 ISSN: 0079-6107 ISO Abbreviation: Prog. Biophys. Mol. Biol. Publication Date: 2004 Oct |
Date Detail:
|
Created Date: 2004-08-03 Completed Date: 2004-11-09 Revised Date: 2004-11-17 |
Medline Journal Info:
|
Nlm Unique ID: 0401233 Medline TA: Prog Biophys Mol Biol Country: England |
Other Details:
|
Languages: eng Pagination: 235-77 Citation Subset: IM |
Affiliation:
|
Computational Biology Research Center, National Institute of Advanced Industrial Science and Technology, Aomi Frontier Building 17F, 2-43 Aomi, Koto-ku, Tokyo 135-0064, Japan. michael-gromiha@aist.go.jp |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Animals Binding Sites Humans Kinetics Models, Molecular Protein Conformation Protein Folding Protein Structure, Secondary Proteins / chemistry*, metabolism* Solvents |
| Chemical | |
Reg. No./Substance:
|
0/Proteins; 0/Solvents |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: HERG binding specificity and binding site structure: evidence from a fragment-based evolutionary com...
Next Document: Glutamate-induced deregulation of calcium homeostasis and mitochondrial dysfunction in mammalian cen...