Determination of the Solid-State Conformations of Polyalanine Using Magic-Angle Spinning NMR Spectroscopy

This publication has 25 references indexed in Scilit:

• Simple techniques for the quantification of protein secondary structure by ¹H NMR spectroscopy
  FEBS Letters, 1991
• Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
  Journal of Molecular Biology, 1991
• Combined sample rotation and multiple-pulse NMR spectroscopic studies on protons bonded to nitrogen-14 nuclei in solid amino acids
  The Journal of Physical Chemistry, 1991
• Primary and secondary structures of synthetic polymer systems as studied by 13C N M R spectroscopy
  Progress in Nuclear Magnetic Resonance Spectroscopy, 1990
• Combined rotation and multiple pulse spectroscopy as an analytical proton nuclear magnetic resonance technique for solids
  Analytical Chemistry, 1988
• 1 3C NMR chemical shift and electronic structure of an infinite polymer chain as studied by tight-binding theory within the CNDO/2 framework: Polyethylene and c i s and t r a n s polyacetylenes
  The Journal of Chemical Physics, 1985
• High-resolution carbon-13 NMR study of silk fibroin in the solid state by the cross-polarization-magic angle spinning method. Conformational characterization of silk I and silk II type forms of Bombyx mori fibroin by the conformation-dependent carbon-13 chemical shifts
  Macromolecules, 1984
• Conformational characterization of polypeptides in the solid state as viewed from the conformation-dependent carbon-13 chemical shifts determined by the carbon-13 cross polarization/magic angle spinning method: oligo(L-alanine), poly(L-alanine), copolymers of L- and D-alanines, and copolymers of L-alanine with N-methyl- or N-benzyl-L-alanine
  Macromolecules, 1983
• Secondary structure of peptides. 4: ¹³C‐Nmr CP/MAS investigation of solid oligo‐ and poly(L‐alanines)
  Biopolymers, 1983
• X-ray studies of poly-L-alanine
  Transactions of the Faraday Society, 1956