Photoprotein Aequorin Structure Determination by NMR Spectroscopy

Abstract

The nine month grant period was used to acquire experience making sequence specific assignments of proteins using homo- and heteronuclear 2D-NMR. Assignments were made for approximately 95% of the 1H and 15N atoms of Bacillus subtilis HPr phosphorylated at Serine 46. Attempts to carry out preliminary homonuclear 2D-NMR studies on r-aequorin were unsuccessful due to serious solubility problems encountered with a lyophilized sample of the photoprotein which had been charged with benzyl coelenterazine. Arrangements are underway to obtain a suitable NMR sample for preliminary analysis. A brief discussion of the methodology that will be required to obtain a solution structure of r-aequorin is included.

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Document Details

Document Type
Technical Report
Publication Date
Jul 09, 1993
Accession Number
ADA267066

Entities

People

  • Bruce R Branchini

Organizations

  • Connecticut College

Tags

DTIC Thesaurus Topics

  • Blood Coagulation Factor Inhibitors
  • Chemistry
  • Connecticut
  • Data Acquisition
  • Data Processing
  • Data Sets
  • Freeze Drying
  • Magnetic Resonance
  • Molecular Weight
  • Nuclear Magnetic Resonance
  • Resonance
  • Sequences
  • Spectroscopy
  • Three Dimensional
  • Two Dimensional
  • Universities

Fields of Study

  • Chemistry

Readers

  • Microbial Pathology
  • Molecular Photonics/Laser Physics
  • Molecular and Cellular Biochemistry