[NMR paper] Differences in Conformational Dynamics Between a Viral Polyprotein and Its Processed Products in Functionally Relevant Regions Revealed by Solution-State NMR Spectroscopy
Differences in Conformational Dynamics Between a Viral Polyprotein and Its Processed Products in Functionally Relevant Regions Revealed by Solution-State NMR Spectroscopy
Viruses have evolved numerous strategies to expand protein function despite their limited genetic material, including proteolytic cleavage of polyproteins to obtain proteins with different functions than their precursors. In this way, proteolysis enables temporal control over the viral life cycle by varying the amounts of proteins in competing cleavage pathways. The 72 kD poliovirus polyprotein 3CD is involved in important protein-protein, protein-RNA and protein-lipid interactions in viral...
[NMR paper] Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Structure. 2019 Mar 28;:
Authors: McDonald AJ, Leon DR, Markham KA, Wu B, Heckendorf CF, Schilling K, Showalter HD,...
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04-09-2019 11:33 PM
[ASAP] Coupling Green Fluorescent Protein Expression with Chemical Modification to Probe Functionally Relevant Riboswitch Conformations in Live Bacteria
Coupling Green Fluorescent Protein Expression with Chemical Modification to Probe Functionally Relevant Riboswitch Conformations in Live Bacteria
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00316/20180626/images/medium/bi-2018-003163_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00316
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/Etm4Uq6nj6M
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06-27-2018 01:51 AM
An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution
An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution
Publication date: Available online 12 April 2018
Source:Methods</br>
Author(s): John D. Persons, Shahid N. Khan, Rieko Ishima</br>
This manuscript presents an NMR strategy to investigate conformational differences in protein-inhibitor complexes, when the inhibitors tightly bind to a protein at sub-nanomolar dissociation constants and are highly analogous to each other. Using HIV-1 protease (PR), we previously evaluated amide chemical shift...
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04-13-2018 01:41 PM
[NMR paper] Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
J Am Chem Soc. 2018 Jan 05;:
Authors: Mandala V, Gelenter MD, Hong M
Abstract
The influenza M2 protein forms a tetrameric proton channel that conducts protons from the acidic endosome into the virion by shuttling...
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01-06-2018 11:17 AM
[NMR paper] Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Biochemistry. 2017 Aug 24;:
Authors: Rasquinha JA, Bej A, Dutta S, Mukherjee S
Abstract
Mutations in p53's DNA binding domain (p53DBD) are associated with 50% of all cancers, making it an essential system to investigate in order to understand the...
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08-25-2017 05:31 PM
[NMR paper] NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
Structure. 2017 Mar 07;25(3):446-457
Authors: Chadwick AC, Jensen DR, Hanson PJ, Lange PT, Proudfoot SC, Peterson FC, Volkman BF, Sahoo D
...
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08-25-2017 04:11 AM
[NMR paper] Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full.gif Related Articles Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2015 Mar 17;112(11):3374-9
Authors: Deshmukh L, Ghirlando R, Clore GM
Abstract
Assembly and maturation of the human...
Differences in Conformational Dynamics Between a Viral Polyprotein and Its Processed Products in Functionally Relevant Regions Revealed by Solution-State NMR Spectroscopy
Linear Mode
