FTIR and NMR studies on the hydration of a high-Mr subunit of glutenin

This publication has 31 references indexed in Scilit:

• Amide modes and protein conformation
  Published by Elsevier ,2003
• New insight into protein secondary structure from resolution-enhanced infrared spectra
  Published by Elsevier ,2003
• 1H NMR relaxation time studies of the hydration of the barley protein C-hordein
  Journal of the Chemical Society, Faraday Transactions, 1994
• Factors affecting the line widths and signal‐to‐noise ratios of the ¹³C CP/MAS spectra of proteins
  Magnetic Resonance in Chemistry, 1993
• Characterization of β‐turns in cyclic hexapeptides in solution by fourier transform IR spectroscopy
  Biopolymers, 1993
• Small-angle X-ray scattering study by synchrotron orbital radiation reveals that high molecular weight subunit of glutenin is a very anisotropic molecule
  Biochemical and Biophysical Research Communications, 1992
• Conformation of wheat gluten proteins Comparison between functional and solution states as determined by infrared spectroscopy
  FEBS Letters, 1992
• NMR transverse relaxation function calculated for constrained polymer chains: application to entanglements and networks
  Macromolecules, 1990
• Carbon-13 NMR of glycogen: hydration response studied by using solids methods
  Biochemistry, 1989
• Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics
  Protein Journal, 1988