Related ArticlesNMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state.
Biomol NMR Assign. 2017 Sep 20;:
Authors: Wang J, Bains H, Anastasia A, Bracken C
Abstract
Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone (1)H, (13)C, and (15)N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2*M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.
PMID: 28933046 [PubMed - as supplied by publisher]
[NMR paper] Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Biomol NMR Assign. 2013 Jul 14;
Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST
Abstract
YibK is a tRNA methyltransferase from Haemophilus influenzae, which forms a stable homodimer in solution and contains a deep trefoil 31 knot encompassing the C-terminal helix that threads through a long loop. It has been a model system for investigating knotted...
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[NMR paper] Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Related Articles Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
Biomol NMR Assign. 2013 Jul 3;
Authors: Hsieh SJ, Mallam AL, Jackson SE, Hsu ST
Abstract
YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent...
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[NMR paper] Structural and dynamic characterization of the urea denatured state of the immunoglob
Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.
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 Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal...
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[NMR paper] A comparison of the pH, urea, and temperature-denatured states of barnase by heteronu
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
J Mol Biol. 1995 Nov 24;254(2):305-21
Authors: Arcus VL, Vuilleumier S, Freund SM, Bycroft M, Fersht AR
The denatured states of...
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[NMR paper] 1H, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topolog
1H, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3.
Related Articles 1H, 13C, and 15N NMR resonance assignments, secondary structure, and backbone topology of a variant of human interleukin-3.
Biochemistry. 1995 May 16;34(19):6540-51
Authors: Feng Y, Klein BK, Vu L, Aykent S, McWherter CA
Interleukin-3 (IL-3) is a cytokine which stimulates the proliferation and differentiation of hematopoietic progenitors into multiple cell lineages. The 1H, 15N, and 13C NMR resonances of...
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[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
J Biomol NMR. 1994 Nov;4(6):845-58
Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD
The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...
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[NMR paper] NMR determination of residual structure in a urea-denatured protein, the 434-represso
NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Related Articles NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
Science. 1992 Sep 11;257(5076):1559-63
Authors: Neri D, Billeter M, Wider G, Wüthrich K
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain...
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[NMR paper] Solid-state NMR triple-resonance backbone assignments in a protein.
Solid-state NMR triple-resonance backbone assignments in a protein.
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J Biomol NMR. 1999 Apr;13(4):337-42
Authors: Tan WM, Gu Z, Zeri AC, Opella SJ
Triple-resonance solid-state NMR spectroscopy is demonstrated to sequentially assign the 13C' and 15N amide backbone resonances of adjacent residues in an oriented protein sample. The observed 13C' chemical shift frequency provides an orientational constraint complementary to those measured from the 1H and 15N amide...