Fractal Surfaces of Proteins
- 6 December 1985
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 230 (4730) , 1163-1165
- https://doi.org/10.1126/science.4071040
Abstract
Fractal surfaces can be used to characterize the roughness or irregularity of protein surfaces. The degree of irregularity of a surface may be described by the fractal dimension D. For protein surfaces defined with probes in the range of 1.0 to 3.5 angstroms in radius, D is approximately 2.4 or intermediate between the value for a completely smooth surface (D = 2) and that for a completely space-filling surface (D = 3). Individual regions of proteins show considerable variation in D. These variations may be related to structural features such as active sites and subunit interfaces, suggesting that surface texture may be a factor influencing molecular interactions.Keywords
This publication has 12 references indexed in Scilit:
- Three-dimensional structure of an antigen–antibody complex at 6 Å resolutionNature, 1985
- The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a proteinNature, 1984
- Correlation between segmental mobility and the location of antigenic determinants in proteinsNature, 1984
- Molecular fractal surfacesNature, 1984
- Analytical molecular surface calculationJournal of Applied Crystallography, 1983
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982
- Protein conformation from electron spin relaxation dataBiophysical Journal, 1982
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- A simplified representation of protein conformations for rapid simulation of protein foldingJournal of Molecular Biology, 1976
- Crystal structure of a lysozyme-tetrasaccharide lactone complexJournal of Molecular Biology, 1974