Structure-function relationships in proteins refer to a trade-off between stability and bioactivity, molded by evolution of the molecule. Identifying which protein amino acid residues jeopardize global or local stability for the benefit of bioactivity would reveal residues pivotal to this structure-function trade-off. Here, we use ^(15)N-¹H heteronuclear single quantum coherence (HSQC) nuclear magnetic resonance (NMR) spectroscopy to probe the microenvironment and dynamics of residues in...
[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...
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[NMR paper] Selective 1Halpha NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs: characterization of minor forms, effects of phosphorylation and occurrence in proteome
Selective 1Halpha NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs: characterization of minor forms, effects of phosphorylation and occurrence in proteome
Identification of proline cis/trans isomers appearing in several regulatory mechanisms of proteins and characterization of minor species present due to the conformational heterogeneity in IDPs is highly important. To obtain residue level information on these mobile systems we introduce two 1 H ? -detected, proline selective, real-time homodecoupled NMR experiments and analyze the proline abundant...
[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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[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
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http://feeds.feedburner.com/~r/acs/bichaw/~4/Etm4Uq6nj6M
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06-27-2018 01:51 AM
[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related Articles Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4248-4251
Authors: Wirmer J, Kühn T, Schwalbe H
Abstract
Aspects of the structure of the intermediate populated after 200 ms in the Ca2+ -induced refolding of ?-lactalbumin have been...
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05-03-2018 06:46 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
Tryptophan-Rich Sensory Protein/Translocator Protein(TSPO) from Cyanobacterium Fremyella diplosiphon Bindsa Broad Range of Functionally Relevant Tetrapyrroles
Tryptophan-Rich Sensory Protein/Translocator Protein(TSPO) from Cyanobacterium Fremyella diplosiphon Bindsa Broad Range of Functionally Relevant Tetrapyrroles
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01019/20161216/images/medium/bi-2016-01019r_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01019
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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NMR Reveals Functionally Relevant Thermally Induced Structural Changes within the Native Ensemble of G-CSF
Linear Mode
