Location of domains in globular proteins
- 1 May 1981
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 291 (5810) , 85-87
- https://doi.org/10.1038/291085a0
Abstract
Although it has become widely accepted that domains are the basic units of structure, function and evolution in proteins, and it is thought that proteins with complex functions evolve by fusion of genes coding for individual domains, the domains are not uniformly defined. Most commonly, domains are simply the compact and more or less loosely connected areas apparent from a visual inspection of protein models. An alternative interpretation is that domains are stable protein fragments found in biochemical experiments. They can be regarded as globular fragments which may refold autonomously and carry specific functions. A method is proposed for location of these globular fragments based on surface area measurements. Applied to several proteins, the globular fragments found often coincide with structural domains or are contained within them.Keywords
This publication has 34 references indexed in Scilit:
- Analytical approximation to the accessible surface area of proteinsProceedings of the National Academy of Sciences, 1980
- Hierarchic organization of domains in globular proteinsJournal of Molecular Biology, 1979
- Refolding of the Immunoglobulin Light Chain1The Journal of Biochemistry, 1979
- Principles of Protein StructurePublished by Springer Nature ,1979
- Stability of Proteins Small Globular ProteinsAdvances in Protein Chemistry, 1979
- The tree structural organization of proteinsJournal of Molecular Biology, 1978
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974
- Equilibrium and kinetics of the denaturation of a homogeneous human immunoglobulin light chainBiochemistry, 1973
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973
- THE COVALENT STRUCTURE OF AN ENTIRE γG IMMUNOGLOBULIN MOLECULEProceedings of the National Academy of Sciences, 1969