Related ArticlesNMR backbone resonance assignment of New Delhi metallo-beta-lactamase.
Biomol NMR Assign. 2017 Aug 14;:
Authors: Yao C, Wu Q, Xu G, Li C
Abstract
The emerging of the New Delhi metallo-beta-lactamase (NDM-1) has become one of the greatest threats to the clinical treatment. Although the structure of NDM-1 has been determined by X-ray crystallography, the molecular mechanism and process of catalysis reaction remain elusive. NMR spectroscopy plays a unique role in the characterization of conformational dynamics. Here we report the backbone (1)H, (15)N and (13)C chemical shift assignments of NDM-1 by heteronuclear multidimensional NMR spectroscopy as well as its secondary structure in solution as predicted by TALOS+.
PMID: 28808891 [PubMed - as supplied by publisher]
[NMR paper] (19) F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-?-Lactamase.
(19) F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-?-Lactamase.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles (19) F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-?-Lactamase.
Angew Chem Int Ed Engl. 2017 Mar 02;:
Authors: Abboud MI, Hinchliffe P, Brem J, Macsics R, Pfeffer I, Makena A, Umland KD, Rydzik AM, Li GB, Spencer J, Claridge TD,...
[NMR paper] Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
Real-Time Monitoring of New Delhi Metallo-?-Lactamase Activity in Living Bacterial Cells by (1) H NMR Spectroscopy.
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Angew Chem Int Ed Engl. 2014 Jan 23;
Authors: Ma J, McLeod S, Maccormack K, Sriram S, Gao N, Breeze AL, Hu J
Abstract
Disconnections between in vitro responses and those observed in whole cells confound many attempts to design drugs in areas of serious medical need. A method based on 1D (1) H...
RDC derived protein backbone resonance assignment using fragment assembly
RDC derived protein backbone resonance assignment using fragment assembly
Abstract Experimental residual dipolar couplings (RDCs) in combination with structural models have the potential for accelerating the protein backbone resonance assignment process because RDCs can be measured accurately and interpreted quantitatively. However, this application has been limited due to the need for very high-resolution structural templates. Here, we introduce a new approach to resonance assignment based on optimal agreement between the experimental and calculated RDCs from a structural template that...
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[NMR paper] GANA--a genetic algorithm for NMR backbone resonance assignment.
GANA--a genetic algorithm for NMR backbone resonance assignment.
Related Articles GANA--a genetic algorithm for NMR backbone resonance assignment.
Nucleic Acids Res. 2005;33(14):4593-601
Authors: Lin HN, Wu KP, Chang JM, Sung TY, Hsu WL
NMR data from different experiments often contain errors; thus, automated backbone resonance assignment is a very challenging issue. In this paper, we present a method called GANA that uses a genetic algorithm to automatically perform backbone resonance assignment with a high degree of precision and recall....
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[NMR paper] NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its
NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Related Articles NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Biochemistry. 1999 Nov 2;38(44):14507-14
Authors: Scrofani SD, Chung J, Huntley JJ, Benkovic SJ, Wright PE, Dyson HJ
Understanding the structure and dynamics of the enzymes that mediate antibiotic resistance of...
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[NMR paper] Complete resonance assignment for the polypeptide backbone of interleukin 1 beta usin
Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Related Articles Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1990 Apr 10;29(14):3542-56
Authors: Driscoll PC, Clore GM, Marion D, Wingfield PT, Gronenborn AM
The complete sequence-specific assignment of the 15N and 1H backbone resonances of the NMR spectrum of recombinant human interleukin 1 beta (153...
NMR backbone resonance assignment of New Delhi metallo-beta-lactamase.
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