NMR provides fresh atomic insights into a key protein that helps repair DNA domain-B
In a new study published in Nature Communications, two teams of scientists from Imperial College London and the University of Dundee have succeeded in visualising this flexible protein for the first time, using Nuclear Magnetic Resonance (NMR) ...
NMR provides fresh atomic insights into a key protein that helps repair DNA - domain-B More...
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NMR provides fresh atomic insights into a key protein that helps repair DNA - Imperial College London
NMR provides fresh atomic insights into a key protein that helps repair DNA - Imperial College London
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NMR provides fresh atomic insights into a key protein that helps repair DNA
Imperial College London
Scientists have made an important advance in understanding how a protein that identifies and repairs cancerous cells operates. RNF4 is a type of regulatory protein that controls the function and fate of proteins in cells by chemically flagging them ...
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Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Dmitry M. Korzhnev, Robert M. Vernon, Tomasz L. Religa, Alexandar L. Hansen, David Baker, Alan R. Fersht and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203686t/aop/images/medium/ja-2011-03686t_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja203686t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-29-2011 04:45 AM
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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06-07-2011 11:05 AM
[NMR paper] Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fra
Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219).
Related Articles Human nucleotide excision repair protein XPA: NMR spectroscopic studies of an XPA fragment containing the ERCC1-binding region and the minimal DNA-binding domain (M59-F219).
Mutat Res. 2001 Jun 5;486(1):1-10
Authors: Buchko GW, Isern NG, Spicer LD, Kennedy MA
XPA is a central protein component of nucleotide excision repair (NER), a ubiquitous,...
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11-19-2010 08:32 PM
[NMR paper] Human nucleotide excision repair protein XPA: expression and NMR backbone assignments
Human nucleotide excision repair protein XPA: expression and NMR backbone assignments of the 14.7 kDa minimal damaged DNA binding domain (Met98-Phe219).
Related Articles Human nucleotide excision repair protein XPA: expression and NMR backbone assignments of the 14.7 kDa minimal damaged DNA binding domain (Met98-Phe219).
J Biomol NMR. 1997 Oct;10(3):313-4
Authors: Buchko GW, Ni S, Thrall BD, Kennedy MA
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[NMR paper] Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a syn
Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
Related Articles Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
J Biomol Struct Dyn. 1997 Jun;14(6):677-90
Authors: Buchko GW, Kennedy MA
A peptide corresponding to residues 101-141 of the human nucleotide excision repair protein XPA was synthesized with an isoleucine...
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08-22-2010 03:31 PM
[NMR paper] Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a syn
Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
Related Articles Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
J Biomol Struct Dyn. 1997 Jun;14(6):677-90
Authors: Buchko GW, Kennedy MA
A peptide corresponding to residues 101-141 of the human nucleotide excision repair protein XPA was synthesized with an isoleucine...