Structural Studies of Metalloprotein Design

Abstract

This project utilized the zinc enzyme human carbonic anhydrase II (CAII) as a paradigm for dissecting and understanding the structural basis of protein transition metal recognition and discrimination. We have successfully redesigned the zinc binding site of CAII so that protein-metal affinity can be modulated by design, by factors of 10 from micromolar to femtomolar affinity. Additionally, our work has illuminated the structural basis of metal binding kinetics, a prerequisite for the development and deployment of a metal ion biosensor.

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Document Details

Document Type
Technical Report
Publication Date
Feb 02, 1999
Accession Number
ADA360687

Entities

People

  • David W. Christianson

Organizations

  • University of Pennsylvania

Tags

Communities of Interest

  • Energy and Power Technologies

DTIC Thesaurus Topics

  • Amides
  • Amino Acids
  • Biochemistry
  • Biosensors
  • Chemical Compounds
  • Chemical Synthesis
  • Chemistry
  • Deployment
  • Energy Transfer
  • Engineering
  • Fluorescence
  • Hydrogen
  • Hydrogen Bonds
  • Kinetics
  • Metalloproteins
  • Molecules
  • Proteins

Fields of Study

  • Chemistry

Readers

  • Molecular and Cellular Biochemistry

Technology Areas

  • Biotechnology