Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and...
[NMR paper] NMR Relaxation Dispersion Experiments to Study Phosphopeptide Recognition by SH2 Domains: The Grb2-SH2-Phosphopeptide Encounter Complex
NMR Relaxation Dispersion Experiments to Study Phosphopeptide Recognition by SH2 Domains: The Grb2-SH2-Phosphopeptide Encounter Complex
Protein interactions are at the essence of life. Proteins evolved not to have stable structures, but rather to be specialized in participating in a network of interactions. Every interaction involving proteins comprises the formation of an encounter complex, which may have two outcomes: (i) the dissociation or (ii) the formation of the final specific complex. Here, we present a methodology to characterize the encounter complex of the Grb2-SH2 domain with a...
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09-06-2023 01:37 AM
[ASAP] Methyl-Based NMR Spectroscopy Methods for Uncovering Structural Dynamics in Large Proteins and Protein Complexes
Methyl-Based NMR Spectroscopy Methods for Uncovering Structural Dynamics in Large Proteins and Protein Complexes
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00953/20181026/images/medium/bi-2018-00953s_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00953
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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11-25-2018 06:02 AM
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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03-01-2013 05:20 PM
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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11-22-2012 11:49 AM
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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10-12-2012 09:58 AM
[NMR paper] Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
From Mendeley Biomolecular NMR group:
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.
Biochemistry (1994). Volume: 33, Issue: 19. Pages: 5984-6003. N a Farrow, R Muhandiram, a U Singer, S M Pascal, C M Kay, G Gish, S E Shoelson, T Pawson, J D Forman-Kay, L E Kay et al.
The backbone dynamics of the C-terminal SH2 domain of phospholipase C gamma 1 have been investigated. Two forms of the domain were studied, one in complex with a high-affinity binding peptide derived from the platelet-derived growth factor receptor and the...
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08-24-2012 08:01 PM
[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
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08-22-2010 03:33 AM
[NMR paper] Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'
Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study.
Protein Sci. 1994 Jul;3(7):1020-30
...
NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes
Linear Mode
