|Dept:||Biochemistry/Biophysics & Molc Biol-AGLS|
|NCBI||Complete Bibliography of Published Work – (Robert Jernigan)|
Director of the Laurence H. Baker Center for Bioinformatics & Biological Statistics. Computational studies on the structures of proteins, nucleic acids, and small molecules, and their interactions. Overall the direction of his research has been to push toward the comprehension of the functions of large structures. Applications are sometimes made to develop molecular models and to select new drugs.
Protein Datamining is used to assess protein structures and their folding patterns. We have evaluated interactions from available structures and other experimental data. We developed a standard way to view interaction energies between residues, based on sets of protein structures. This approach led to useful ways to incorporate structural and hydrophobicity information into simulations.
Conformation Generation. We developed a new approach to enumerate protein lattice conformations with full efficiency. This is particularly important for determining native protein conformations, where the problem is akin to searching for a needle in a haystack, and random searches are largely ineffective. This new approach opens the way for the computer generation of much larger numbers of protein conformations.
Elastic models of Proteins. Large-domain motions of proteins are computed with simple inter-connected elastic models. These highly cohesive, cooperative models are most appropriate for considering the largest functional motions of proteins, which are necessarily independent of the structural details. Functional mechanisms for processing proteins or for protein machines can be developed. The methods lend themselves in straightforward ways to the investigation of the motions of extremely large biomolecular assemblages of more than 100,000 residues.
- B.S., Chemistry, California Institute of Technology, 1963
Ph.D., Physical Chemistry, Stanford University, 1967
Postdoctoral Fellow, University of California – San Diego