Solvent and temperature effects on crambin, a hydrophobic protein, as investigated by proton magnetic resonance

Eur J Biochem. 1981 Oct;119(3):483-90. doi: 10.1111/j.1432-1033.1981.tb05633.x.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Magnetic Resonance Spectroscopy
  • Plant Proteins*
  • Proteins / analysis*
  • Protons
  • Solvents
  • Temperature

Substances

  • Plant Proteins
  • Proteins
  • Protons
  • Solvents
  • crambin protein, Crambe abyssinica