The Neutron Structure of the Hydrophobic Plant Protein Crambin

  • Martha M. Teeter
  • Anthony A. Kossiakoff
Chapter
Part of the Basic Life Sciences book series (BLSC, volume 27)

Abstract

Crystals of the small Hydrophobic protein crambin have been shown to diffract to a resolution of at least 0.88 Å (11). This means that crambin presents a rare opportunity to study a protein structure at virtually atomic resolution. The high resolution of the diffraction pattern coupled with the assets of neutron diffraction present the distinct possibility that crambin’s analysis may surpass that of any other protein system in degree and accuracy of detail.

Keywords

Neutron Diffraction Amide Proton Deuterium Atom Peptide Proton Water Oxygen Atom 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Martha M. Teeter
    • 1
  • Anthony A. Kossiakoff
    • 2
  1. 1.Dept. of ChemistryBoston UniversityBostonUSA
  2. 2.Biology Dept.Brookhaven National LaboratoryUptonUSA

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