A comprehensive and comparative study of the internal structure and dynamics of natural ß-keratin and regeneratedß-keratin by solid state NMR spectroscopy.
Solid State Nucl Magn Reson
; 101: 1-11, 2019 09.
Article
en En
| MEDLINE
| ID: mdl-31055225
Structure and dynamics of natural and regenerated chicken feather ß-keratin were investigated by 13C cross-polarization (CP) magic angle spinning (MAS) solid state nuclear magnetic resonance (SSNMR) spectral analysis, 13C and 1H spin-lattice relaxation time measurements, and 13C two dimensional phase adjusted spinning sidebands (2DPASS) MAS SSNMR measurements. Chemical shift anisotropy (CSA) parameters of both natural and regenerated chicken feather ß-keratin were extracted by using 2DPASS MAS SSNMR experiment. The beauty of 2DPASS MAS SSNMR experiment is it can correlate the isotropic and anisotropic dimension with the help of shearing transformation and two dimensional Fourier Transformation. Molecular correlation time at each and every magnetically inequivalent carbon site of both natural and regenerated chicken feather ß-keratin were also determined. The change in molecular dynamics of structural protein after pretreatment was monitored by 2DPASS MAS SSNMR and 13C relaxation measurement. This type of comprehensive study will provide the information about the interrelation between the structure and dynamics of structural protein and will also shed light in the way of developing methods for conversion of animal by-products to novel product.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Resonancia Magnética Nuclear Biomolecular
/
Beta-Queratinas
Límite:
Animals
Idioma:
En
Revista:
Solid State Nucl Magn Reson
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Año:
2019
Tipo del documento:
Article
Pais de publicación:
Países Bajos