[NMR paper] A comprehensive and comparative study of the internal structure and dynamics of natural ?-keratin and regenerated?-keratin by solid state NMR spectroscopy.
A comprehensive and comparative study of the internal structure and dynamics of natural ?-keratin and regenerated?-keratin by solid state NMR spectroscopy.
Related ArticlesA comprehensive and comparative study of the internal structure and dynamics of natural ?-keratin and regenerated?-keratin by solid state NMR spectroscopy.
Solid State Nucl Magn Reson. 2019 Apr 26;101:1-11
Authors: Ghosh M, Prajapati BP, Kango N, Dey KK
Abstract
Structure and dynamics of natural and regenerated chicken feather ?-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 ?-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 ?-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.
PMID: 31055225 [PubMed - as supplied by publisher]
[NMR paper] A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.
A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.
Related Articles A Comparative Study of Secondary Structure and Interactions of the R5 Peptide in Silicon Oxide and Titanium Oxide Co-precipitates using Solid-state NMR Spectroscopy.
Langmuir. 2017 Sep 12;:
Authors: Buckle EL, Roehrich A, Vandermoon B, Drobny GP
Abstract
A biomimetic, peptide-mediated approach to inorganic nanostructure formation is of great interest...
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09-13-2017 08:48 PM
Solid state NMR of isotope labelled murine fur: a powerful tool to study atomic level keratin structure and treatment effects
Solid state NMR of isotope labelled murine fur: a powerful tool to study atomic level keratin structure and treatment effects
Abstract
We have prepared mouse fur extensively 13C,15N-labelled in all amino acid types enabling application of 2D solid state NMR techniques which establish covalent and spatial proximities within, and in favorable cases between, residues. 13C double quantumâ??single quantum correlation and proton driven spin diffusion techniques are particularly useful for resolving certain amino acid types. Unlike 1D experiments on...
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11-19-2016 08:35 PM
[NMR paper] NMR spectroscopy reveals the presence and association of lipids and keratin in adhesive gecko setae.
NMR spectroscopy reveals the presence and association of lipids and keratin in adhesive gecko setae.
Related Articles NMR spectroscopy reveals the presence and association of lipids and keratin in adhesive gecko setae.
Sci Rep. 2015;5:9594
Authors: Jain D, Stark AY, Niewiarowski PH, Miyoshi T, Dhinojwala A
Abstract
Lipid and protein aggregates are one of the fundamental materials of biological systems. Examples include cell membranes, insect cuticle, vertebrate epidermis, feathers, hair and adhesive structures known as 'setae' on...
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04-23-2015 06:11 PM
[NMR paper] Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
Related Articles Internal protein dynamics on ps to ?s timescales as studied by multi-frequency (15)N solid-state NMR relaxation.
J Biomol NMR. 2013 Sep 19;
Authors: Zinkevich T, Chevelkov V, Reif B, Saalwächter K, Krushelnitsky A
Abstract
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09-21-2013 06:50 PM
[NMR paper] Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Solid-State NMR Approaches to Internal Dynamics of Proteins: From Picoseconds to Microseconds and Seconds.
Acc Chem Res. 2013 Jul 23;
Authors: Krushelnitsky A, Reichert D, Saalwächter K
Abstract
Solid-state nuclear magnetic resonance (NMR) spectroscopy has matured to the point that it is possible to determine the structure of proteins in immobilized states, such as within microcrystals or embedded in membranes. Currently, researchers...
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07-24-2013 04:52 PM
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
J Am Chem Soc. 2011 Jan 5;
Authors: Li S, Hong M
Histidine structure and chemistry lie at the heart of many enzyme active sites, ion channels, and metalloproteins. While solid-state NMR spectroscopy has been used to study histidine chemical shifts, the full pH dependence of the...
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01-07-2011 11:21 PM
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Shenhui Li and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108943n/aop/images/medium/ja-2010-08943n_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108943n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/FuFM0C9qHyE
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01-05-2011 11:40 PM
Comprehensive Solid-State NMR Characterization of Electronic Structure in Ditechnetiu
Comprehensive Solid-State NMR Characterization of Electronic Structure in Ditechnetium Heptoxide
Herman Cho et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja105687j/aop/images/medium/ja-2010-05687j_0002.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
A comprehensive and comparative study of the internal structure and dynamics of natural ?-keratin and regenerated?-keratin by solid state NMR spectroscopy.
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