Printer Friendly

The texture of clinging proteins.

The varying roughness of a protein molecule's convoluted surface may influence how different parts of the protein interact with other molecules. One way to describe the roughness of such an irregular surface is to measure and compute its fractal dimension (SN: 1/21/84, p. 42). A perfectly smooth surface has a fractal dimension of 2, while an extremely rough surface with features that fill all of space has a dimension of 3.

In the Dec. 6 SCIENCE, Mitchell Lewis of SmithKline and French Laboratories in Philadelphia and D.C. Rees of the University of California at Los Angeles report that the fractal dimension of several protein surfaces is about 2.4. This dimension, however, varies considerably from place to place along a given protein. Because the amount of surface detail detected depends on the size of the probe used, these results apply for probes in the range of 1.0 to 3.5 angstroms in radius.

For proteins like lysozyme and superoxide dismutase, regions involved in the formation of tight complexes, in which molecules are firmly bound together, appear to be more irregular than average. Regions known as active sites, which are involved in the formation of transient complexes, seem to be smoother than average.

"These considerations suggest that the calculation of fractal surfaces...may be a useful technique," Lewis and Rees conclude. "Recognition of these geometric factors provides a new approach to describing the interaction of macromolecules with one another."
COPYRIGHT 1985 Science Service, Inc.
No portion of this article can be reproduced without the express written permission from the copyright holder.
Copyright 1985, Gale Group. All rights reserved. Gale Group is a Thomson Corporation Company.

Article Details
Printer friendly Cite/link Email Feedback
Title Annotation:research on fractal dimension of protein molecules
Publication:Science News
Date:Dec 14, 1985
Words:242
Previous Article:A solid look at xenon.
Next Article:T-PA as stroke treatment?
Topics:


Related Articles
Redesigning molecules nature's way.
Unraveling the biochemistry of spider silk.
Analyzing protein cocktails in a snap.
Relate structure, rheology to interparticle interactions and gelation.
Relate structure, rheology to interparticle interactions and gelation.
Proteins in the stretch: tugging at single molecules reveals their secrets.
Interparticle interactions and gelation impact structure, rheology.
Risk factor: throat cancer linked to virus spread by sex.
Alzheimer's marker yields blood test.
High on conservation: this Washington state forest ecologist and professor shares her research, and her convictions, literally from the treetops.

Terms of use | Copyright © 2017 Farlex, Inc. | Feedback | For webmasters