Accession Number:

ADA220926

Title:

A Modular Approach to Protein Design

Descriptive Note:

Annual rept. 1 Feb 1989-1 Mar 1990

Corporate Author:

ROCHESTER UNIV NY

Personal Author(s):

Report Date:

1990-04-16

Pagination or Media Count:

5.0

Abstract:

We have taken a modular approach to design peptides which adopt defined structures and perform specific tasks. Peptides are being designed to bind either a specific sequence of double stranded DNA of the pp561ck tyrosine protein kinase which likely is the cytoplasmic effector of a transmembrane receptor whose activation in vivo is associated with an increase in cytoplasmic free calcium. Peptides have been synthesized which bind to each of these macromolecules with KDs near 2uM. In addition to binding pp561ck tightly, one peptide has been found to stimulate the activity of this enzyme up to 20-fold. Initial results suggest that ionic interactions are important for this activation. Currently work is continuing on both projects. DNA binding peptides are being redesigned to maximize their ability to discriminate between different nucleotide sequences.

Subject Categories:

  • Genetic Engineering and Molecular Biology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE