Extended DNA amplification with thermostable chaperons
Award last edited on: 2/22/05

Sponsored Program
Awarding Agency
Total Award Amount
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Principal Investigator
Frank Robb

Company Information

Fidelity Systems Inc

7961 Cessna Avenue
Gaithersburg, MD 20879
   (301) 527-0804

Research Institution

University of Maryland Biotech Institute

Phase I

Contract Number: 1R41GM073295-01
Start Date: 00/00/00    Completed: 00/00/00
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The goal of this project is to develop a general method of improving the stability and durability of enzymes used in DNA and RNA amplification, sequencing, restriction analysis and ligation. The enzymes to be improved include DNA polymerases, topoisomerases, reverse transcriptases and ligases. In the event this goal can be achieved, broad impacts may result in the areas of clinical, forensic and basic science that rely on DNA sequencing, amplification and RT-PCR processes. To do this, extrinsic stabilization and refolding of proteins mediated by chaperones from hyperthermophiles will be adapted for incorporation into reaction mixtures with DNA modifying enzymes.

Thesaurus Terms:
DNA, DNA directed DNA polymerase, molecular chaperone, nucleic acid amplification technique, nucleic acid sequence, protein engineering, synthetic enzyme, thermostability DNA topoisomerase, RNA directed DNA polymerase, chemical reaction, enzyme activity, enzyme structure, ligase, nucleic acid denaturation, protein folding biotechnology, high throughput technology, polymerase chain reaction

Phase II

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Start Date: 00/00/00    Completed: 00/00/00
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