Hydrogen-Bonding Structure of Serine Side Chains in Bombyx mori and Samia cynthia ricini Silk Fibroin Determined by Solid-State 2H NMR
- 15 September 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Macromolecules
- Vol. 32 (21) , 7166-7171
- https://doi.org/10.1021/ma990554q
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Structural analysis of uniaxially aligned polymers using solid-state nitrogen-15 NMRMacromolecules, 1993
- A method for studying the structure of uniaxially aligned biopolymers using solid state 15N‐nmr: Application to Bombyx mori silk fibroin fibersBiopolymers, 1993
- 2H NMR lineshapes of immobilized uniaxially oriented membrane proteinsSolid State Nuclear Magnetic Resonance, 1993
- 1H pulsed NMR study of bombyx mori silk fibroin: Dynamics of fibroin and of absorbed waterJournal of Polymer Science Part B: Polymer Physics, 1992
- Dynamic features of side chains in tyrosine and serine residues of some polypeptides and fibroins in the solid as studied by high-resolution solid-state carbon-13 NMR spectroscopyMacromolecules, 1990
- A2H NMR Study of [Ser-3,3-2H2]- and [Ala-3,3,3-2H3]- Silk Fibroins in the Solid State. Role of Side-Chain Moiety in Stabilization of Secondary StructureBulletin of the Chemical Society of Japan, 1986
- Intrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices and its relevance to membrane-bound proteinsJournal of Molecular Biology, 1984
- Orientational distribution of polymer chains studied by 2H n.m.r. line shapesPolymer, 1981
- The amino-terminal sequence of silk fibroin peptide Cp — A reinvestigationBiochemical and Biophysical Research Communications, 1977
- An investigation of the structure of silk fibroinBiochimica et Biophysica Acta, 1955