A Modular Approach to Protein Design

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.

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Document Details

Document Type
Technical Report
Publication Date
Apr 16, 1990
Accession Number
ADA220926

Entities

People

  • H. N. Bramson

Organizations

  • University of Rochester

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Cell Physiological Processes
  • Contracts
  • Enzymes
  • Kinases
  • Lymphocytes
  • Macromolecules
  • Military Research
  • Molecules
  • Protein-Protein Interactions
  • Regulations
  • Ribonuclease
  • Sequences
  • Small Molecules
  • Tyrosine
  • Universities

Fields of Study

  • Biology

Readers

  • Computer Science.
  • Molecular Genetics
  • Molecular and Cellular Biochemistry