[NMR paper] Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study
Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study
Wheat germ agglutinin (WGA) demonstrates potential as an oral delivery agent owing to its selective binding to carbohydrates and its capacity to traverse biological membranes. In this study, we employed differential scanning calorimetry and molecular dynamics simulations to comprehensively characterize the thermal unfolding process of both the complete lectin and its four isolated domains. Furthermore, we present the nuclear magnetic resonance structures of three domains that were previously...
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
From The DNP-NMR Blog:
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
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Oganesyan, V.S., et al., A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics. J. Magn. Reson., 2017. 274: p. 24-35.
www.sciencedirect.com/science/article/pii/S1090780716302270
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[NMR paper] A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
A combined EPR and MD simulation study of a nitroxyl spin label with restricted internal mobility sensitive to protein dynamics
Publication date: January 2017
Source:Journal of Magnetic Resonance, Volume 274</br>
Author(s): Vasily S. Oganesyan, Fatima Chami, Gaye F. White, Andrew J. Thomson</br>
EPR studies combined with fully atomistic Molecular Dynamics (MD) simulations and an MD-EPR simulation method provide evidence for intrinsic low rotameric mobility of a nitroxyl spin label, Rn, compared to the more widely employed label MTSL (R1). Both experimental...
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11-19-2016 08:35 PM
[NMR paper] Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Unfolding the mechanism of the AAA+ unfoldase VAT by a combined cryo-EM, solution NMR study.
Proc Natl Acad Sci U S A. 2016 Jul 11;
Authors: Huang R, Ripstein ZA, Augustyniak R, Lazniewski M, Ginalski K, Kay LE, Rubinstein JL
Abstract
The AAA+ (ATPases associated with a variety of cellular activities) enzymes play critical roles in a variety of homeostatic processes in all kingdoms of life. Valosin-containing protein-like ATPase of...
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07-13-2016 10:14 AM
[NMR paper] Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach.
Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach.
Related Articles Pressure-induced structural transition of mature HIV-1 Protease from a combined NMR/MD simulation approach.
Proteins. 2015 Sep 18;
Authors: Roche J, Louis JM, Bax A, Best RB
Abstract
We investigate the pressure-induced structural changes in the mature human immunodeficiency virus type 1 protease dimer (HIV-1 PR), using residual dipolar coupling (RDC) measurements in a weakly oriented solution. (1) DNH RDCs...
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09-20-2015 12:56 PM
[NMR paper] NMR and molecular modeling studies of the interaction between wheat germ agglutinin a
NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Related Articles NMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Biochemistry. 2004 Aug 3;43(30):9647-54
Authors: Lycknert K, Edblad M, Imberty A, Widmalm G
The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly...
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11-24-2010 10:01 PM
[NMR paper] 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a m
13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface.
Related Articles 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface.
Biochemistry. 1994 Aug 23;33(33):10137-48
Authors: Hare BJ, Rise F, Aubin Y, Prestegard JH
The orientation of synthetic 13C-labeled glycolipid receptors and their interaction with the plant lectin wheat germ agglutinin have been studied in an oriented membrane system using NMR...
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08-22-2010 03:29 AM
Wheat Germ Cell-Free Protein Production Workshop
Wheat Germ Cell-Free Protein Production Workshop
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The Center for Eukaryotic Structural Genomics (CESG) and the Nuclear Magnetic Resonance Facility at Madison
(NMRFAM) are pleased to announce the first Wheat Germ Cell-Free Protein Production Workshop to be held from
July 30 - August 4, 2006, at the Department of Biochemistry at the University of Wisconsin-Madison in Madison, Wisconsin,
USA. To register for this workshop, complete the Registration Form on the next page and mail in with your NONREFUNDABLE