The prediction of protein structure solely from sequence information remains one of the great unsolved problems in computational chemistry. There is now, however, a sufficiently large database of three-dimensional structures that makes it possible to predict a protein's overall topology by solving the inverse of the protein folding problem. That is, given a protein structure, what amino acid sequences are likely to adopt that particular fold?
BIOSYM's Profiles-3D software answers this question using the 3D profile method developed in the laboratory of Dr. David Eisenberg at UCLA. It measures the compatibility of amino acids in a sequence with the physical environments of the residues in the structure.
Brenda Pfeiffer
Marketing Specialist BIOSYM Technologies, Inc. 9685 Scranton Road San Diego, CA 92121-3752 USA 619-546-5319 fax:619-597-9777 blp@biosym.com