Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
J Struct Biol. 2011 Apr 9;
Authors: Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki EI, Shimada I, Takahashi H
Protein-protein interactions are necessary for various cellular...
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04-20-2011 07:15 PM
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...
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11-25-2010 08:21 PM
[NMR paper] The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining pro
The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
Related Articles The fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
J Magn Reson. 2005 Apr;173(2):310-6
Authors: Meiler J, Baker D
We illustrate how moderate resolution protein structures can be rapidly obtained by interlinking computational prediction methodologies with un- or partially assigned NMR data. To...
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11-25-2010 08:21 PM
[NMR paper] Rapid assessment of protein structural stability and fold validation via NMR.
Rapid assessment of protein structural stability and fold validation via NMR.
Related Articles Rapid assessment of protein structural stability and fold validation via NMR.
Methods Enzymol. 2005;394:142-75
Authors: Hoffmann B, Eichmüller C, Steinhauser O, Konrat R
In structural proteomics, it is necessary to efficiently screen in a high-throughput manner for the presence of stable structures in proteins that can be subjected to subsequent structure determination by X-ray or NMR spectroscopy. Here we illustrate that the (1)H chemical...
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11-24-2010 11:14 PM
[NMR paper] Rapid protein fold determination using unassigned NMR data.
Rapid protein fold determination using unassigned NMR data.
Related Articles Rapid protein fold determination using unassigned NMR data.
Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15404-9
Authors: Meiler J, Baker D
Experimental structure determination by x-ray crystallography and NMR spectroscopy is slow and time-consuming compared with the rate at which new protein sequences are being identified. NMR spectroscopy has the advantage of rapidly providing the structurally relevant information in the form of unassigned chemical shifts (CSs),...
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11-24-2010 09:16 PM
CABS-NMR-De novo tool for rapid global fold determination from chemical shifts, resid
CABS-NMR-De novo tool for rapid global fold determination from chemical shifts, residual dipolar couplings and sparse methyl-methyl noes.
CABS-NMR-De novo tool for rapid global fold determination from chemical shifts, residual dipolar couplings and sparse methyl-methyl noes.
J Comput Chem. 2010 Aug 30;
Authors: Latek D, Kolinski A
Recent development of nuclear magnetic resonance (NMR) techniques provided new types of structural restraints that can be successfully used in fast and low-cost global protein fold determination. Here, we present...
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09-02-2010 03:58 PM
[NMR paper] An approach to global fold determination using limited NMR data from larger proteins
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residue types.
J Biomol NMR. 1996 Oct;8(3):360-8
Authors: Smith BO, Ito Y, Raine A, Teichmann S, Ben-Tovim L, Nietlispach D, Broadhurst RW, Terada T, Kelly M, Oschkinat H, Shibata T, Yokoyama S, Laue ED
A combination of calculation and experiment is used to demonstrate that the global fold of...
Rapid protein fold determination using unassigned NMR data
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