Cyril Charlier, Guillaume Bouvignies, Philippe Pelupessy, Astrid Walrant, Rodrigue Marquant, Mikhail Kozlov, Pablo De Ioannes, Nicolas Bolik-Coulon, Sandrine Sagan, Patricia Cortes, Aneel K. Aggarwal, Ludovic Carlier and Fabien Ferrage
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b05823
[NMR paper] Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
Related Articles Structure and dynamics of an intrinsically disordered protein region that partially folds upon binding by chemical-exchange NMR.
J Am Chem Soc. 2017 Aug 07;:
Authors: Charlier C, Bouvignies G, Pelupessy P, Walrant A, Marquant R, Kozlov M, De Ioannes P, Bolik-Coulon N, Sagan S, Cortes P, Aggarwal AK, Carlier L, Ferrage F
Abstract
Many intrinsically disordered proteins (IDPs) and protein...
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08-07-2017 07:31 PM
Structureand Dynamics of the Huntingtin Exon-1N-Terminus: A*Solution NMR Perspective
Structureand Dynamics of the Huntingtin Exon-1N-Terminus: A*Solution NMR Perspective
Maria Baias, Pieter E. S. Smith, Koning Shen, Lukasz A. Joachimiak, Szymon Z?erko, Wiktor Koz?min?ski, Judith Frydman and Lucio Frydman
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b10893/20170113/images/medium/ja-2016-108934_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b10893
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/6vVAqMsGYCM
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01-14-2017 06:24 AM
[NMR paper] Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Related Articles Characterization of the conformational preference and dynamics of the intrinsically disordered N-terminal region of beclin 1 by NMR spectroscopy.
Biochim Biophys Acta. 2016 Jun 8;
Authors: Yao S, Lee EF, Pettikiriarachchi A, Evangelista M, Keizer DW, Fairlie WD
Abstract
Beclin 1 is a 450 amino acid protein that plays critical roles in the early stages of autophagosome...
Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins
Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins
Abstract
There has been a longstanding interest in being able to accurately predict NMR chemical shifts from structural data. Recent studies have focused on using molecular dynamics (MD) simulation data as input for improved prediction. Here we examine the accuracy of chemical shift prediction for intein systems, which have regions of intrinsic disorder. We find that using MD simulation data as input for chemical shift prediction does not...
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11-21-2014 09:04 PM
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
Local protein backbone folds determined by calculated NMR chemical shifts.
J Comput Chem. 2011 Sep 9;
Authors: Czajlik A, Hudáky I, Perczel A
Abstract
NMR chemical shifts (CSs: ?N(NH) , ?C(?) , ?C(?) , ?C', ?H(NH) , and ?H(?) ) were computed for the amino acid backbone conformers (?(L) , ?(L) , ?(L) , ?(L) , ?(L) , ?(D) , ?(D) , ?(D) , and ?(D) ) modeled by oligoalanine structures. Topological differences of the extended fold were investigated on single ?-strands,...
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09-10-2011 06:51 PM
The calponin regulatory region is intrinsically unstructured: novel insight into actin-calponin and calmodulin-calponin interfaces using NMR spectroscopy.
The calponin regulatory region is intrinsically unstructured: novel insight into actin-calponin and calmodulin-calponin interfaces using NMR spectroscopy.
The calponin regulatory region is intrinsically unstructured: novel insight into actin-calponin and calmodulin-calponin interfaces using NMR spectroscopy.
Biophys J. 2011 Apr 6;100(7):1718-28
Authors: Pfuhl M, Al-Sarayreh S, El-Mezgueldi M
Calponin is an actin- and calmodulin-binding protein believed to regulate the function of actin. Low-resolution studies based on proteolysis established that...
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04-06-2011 10:54 AM
[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
Structureand Dynamics of an Intrinsically DisorderedProtein Region That Partially Folds upon Binding by Chemical-ExchangeNMR
Linear Mode
