The proteins that comprise the water-soluble interior of the optic lens are referred to as crystallin proteins, of which three major categories have been identified: alpha (a), beta (b), and gamma (y). Gamma and beta crystallin proteins have been observed to undergo aggregation and phase-separation over time, which can lead to the formation of cataracts, while alpha crystallin limits this formation by removing deformed protein aggregates from solution. Here, we describe our studies on bovine yB...
[NMR paper] Insights to Human gammaD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations
Insights to Human gammaD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations
Human ?D-crystallin (HGDC) is an abundant lens protein residing in the nucleus of the human lens. Aggregation of this and other structural proteins within the lens leads to the development of cataract. Much has been explored on the stability and aggregation of HGDC and where detailed investigation at the atomic resolution was needed, the X-ray structure was used as an initial starting conformer for molecular modeling. In this study, we implemented NMR-solution HGDC structures as starting......
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02-17-2022 11:34 AM
[NMR paper] Residue-Specific Kinetic Insights into the Transition State in Slow Polypeptide Topological Isomerization by NMR Exchange Spectroscopy
Residue-Specific Kinetic Insights into the Transition State in Slow Polypeptide Topological Isomerization by NMR Exchange Spectroscopy
The characterization of the transition state is a central issue in biophysical studies of protein folding. NMR is a multiprobe measurement technique that provides residue-specific information. Here, we used exchange spectroscopy to characterize the transition state of the two-state slow topological isomerization of a 27-residue lantibiotic peptide. The exchange kinetic rates varied on a per-residue basis, indicating the reduced kinetic cooperativity of the...
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10-26-2021 01:10 PM
[NMR paper] Characterizing the Brownian Diffusion of Nanocolloids and Molecular Solutions: Diffusion Ordered NMR Spectroscopy versus Dynamic Light Scattering.
Characterizing the Brownian Diffusion of Nanocolloids and Molecular Solutions: Diffusion Ordered NMR Spectroscopy versus Dynamic Light Scattering.
Related Articles Characterizing the Brownian Diffusion of Nanocolloids and Molecular Solutions: Diffusion Ordered NMR Spectroscopy versus Dynamic Light Scattering.
J Phys Chem B. 2020 May 01;:
Authors: Zhang C, Jin Z, Zeng B, Wang W, Palui G, Mattoussi H
Abstract
Hydrodynamic size is a characteristic dimension that reflects the Brownian diffusion of objects, such as proteins,...
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05-03-2020 02:46 PM
[NMR paper] Comparison of NMR and Dynamic Light Scattering for Measuring Diffusion Coefficients of Formulated Insulin: Implications for Particle Size Distribution*Measurements in Drug Products.
Comparison of NMR and Dynamic Light Scattering for Measuring Diffusion Coefficients of Formulated Insulin: Implications for Particle Size Distribution*Measurements in Drug Products.
Related Articles Comparison of NMR and Dynamic Light Scattering for Measuring Diffusion Coefficients of Formulated Insulin: Implications for Particle Size Distribution*Measurements in Drug Products.
AAPS J. 2017 Aug 08;:
Authors: Patil SM, Keire DA, Chen K
Abstract
Particle size distribution, a measurable physicochemical quantity, is a critical...
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qcs9RnHBiBY
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09-08-2012 08:44 AM
Sequence-Specific Mappingof the Interaction betweenUrea and Unfolded Ubiquitin from Ensemble Analysis of NMR and SmallAngle Scattering Data
Sequence-Specific Mappingof the Interaction betweenUrea and Unfolded Ubiquitin from Ensemble Analysis of NMR and SmallAngle Scattering Data
Jie-rong Huang, Frank Gabel, Malene Ringkjøbing Jensen, Stephan Grzesiek and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2118688/aop/images/medium/ja-2011-118688_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2118688
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/u0K4iYUlStc
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02-23-2012 07:38 AM
[NMR paper] Real-time NMR kinetic studies provide global and residue-specific information on the
Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
Related Articles Real-time NMR kinetic studies provide global and residue-specific information on the non-cooperative unfolding of the beta-trefoil protein, interleukin-1beta.
J Mol Biol. 2003 May 2;328(3):693-703
Authors: Roy M, Jennings PA
The interleukin-1beta (IL-1beta) structural motif is a beta-trefoil super fold created by six two-stranded beta-hairpins. Turns are thus...
Analysis of Global and Residue-Specific yB Crystallin Protein Dynamics via NMR Spectroscopy and Dynamic Light Scattering
Linear Mode
