High-molecular-weight (HMW) hyaluronic acid (HA) is a highly abundant natural polysaccharide and a fundamental component of the extracellular matrix (ECM). Its size and concentration regulate tissues' macro- and microenvironments, and its upregulation is a hallmark feature of certain tumors. Yet, the conformational dynamics of HMW-HA and how it engages with the components of the ECM microenvironment remain poorly understood at the molecular level. Probing the molecular structure and dynamics of...
[NMR paper] Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR
Production of isotopically enriched high molecular weight hyaluronic acid and characterization by solid-state NMR
Hyaluronic acid (HA) is a naturally occurring polysaccharide that is abundant in the extracellular matrix (ECM) of all vertebrate cells. HA-based hydrogels have attracted great interest for biomedical applications due to their high viscoelasticity and biocompatibility. In both ECM and hydrogel applications, high molecular weight (HMW)-HA can absorb a large amount of water to yield matrices with a high level of structural integrity. To understand the molecular underpinnings of...
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[NMR paper] Effects of Pectin Molecular Weight Changes on the Structure, Dynamics, and Polysaccharide Interactions of Primary Cell Walls of Arabidopsis thaliana: Insights from Solid-State NMR.
Effects of Pectin Molecular Weight Changes on the Structure, Dynamics, and Polysaccharide Interactions of Primary Cell Walls of Arabidopsis thaliana: Insights from Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Effects of Pectin Molecular Weight Changes on the Structure, Dynamics, and Polysaccharide Interactions of Primary Cell Walls of Arabidopsis thaliana: Insights from Solid-State NMR.
Biomacromolecules. 2017 Sep 11;18(9):2937-2950
Authors: Phyo P,...
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05-04-2018 03:33 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] Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
Amino Acids. 2013 Mar;44(3):821-33
Authors: Su Y, Li S, Hong M
Abstract
Many membrane-active peptides, such as cationic cell-penetrating peptides (CPPs) and antimicrobial peptides...
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08-15-2013 07:45 PM
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Raquel Godoy-Ruiz, Chenyun Guo and Vitali Tugarinov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1083656/aop/images/medium/ja-2010-083656_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1083656
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hxZ4cabF688
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12-08-2010 10:04 AM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
J Am Chem Soc. 2005 Jun 8;127(22):8214-25
Authors: Tugarinov V, Ollerenshaw JE, Kay LE
New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
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11-25-2010 08:21 PM
[NMR paper] Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR.
Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Related Articles Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Biopolymers. 2002 Oct 15;65(2):158-68
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Naito A, Okuda K, Saitô H, Gil AM
This work follows a previous article that addressed the role of disulfide bonds in...
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11-24-2010 08:58 PM
[NMR paper] Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state
Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Related Articles Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Biopolymers. 2002;67(6):487-98
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Gil AM
This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of...