[NMR paper] A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
Angew Chem Int Ed Engl. 2013 Aug 22;
Authors: Long D, Marshall CB, Bouvignies G, Mazhab-Jafari MT, Smith MJ, Ikura M, Kay LE
Abstract
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09-17-2013 11:36 PM
[NMR paper] Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Feb 28;
Authors: Vallurupalli P, Kay LE
Abstract
Seeing the invisible: A 13 CO NMR chemical exchange saturation transfer (CEST) experiment for the study of "invisible" excited protein states with lifetimes on the order of 5-50 ms has been developed. The 13 CO chemical...
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03-02-2013 11:45 AM
Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead
Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
David Ban, Alvar D. Gossert, Karin Giller, Stefan Becker, Christian Griesinger, Donghan Lee</br>
Internal motions in the microsecond timescale have been proposed to play an active part in a protein’s biological function. Nuclear magnetic resonance (NMR) relaxation dispersion is a robust method sensitive to this timescale with atomic resolution. However, due to technical...
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05-15-2012 06:40 PM
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
Abstract A TROSY-selected ZZ-exchange experiment is described for measuring slow chemical exchange rates by monitoring the TROSY component of 15N longitudinal magnetization. Application of the proposed pulse sequence to the cadherin 8 N-terminal extracelluar domain demonstrates that enhanced sensitivity is obtained, compared to a previously described TROSY-detected ZZ-exchange sequence (Sahu et al. J Am Chem Soc 129: 13232â??13237, 2007), by preserving the TROSY effect during the mixing...
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01-09-2011 12:46 PM
[NMR paper] 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic bindi
19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Related Articles 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Biochemistry. 1992 Aug 11;31(31):7069-76
Authors: Dubois BW, Evers AS
This paper characterizes the low-affinity ligand binding interactions of a fluorinated volatile anesthetic, isoflurane (CHF2OCHClCF3), with bovine serum albumin...
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08-21-2010 11:45 PM
Use of chemical shifts for structural studies of nucleic acids
Use of chemical shifts for structural studies of nucleic acids
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 1 February 2010</br>
Sik Lok, Lam , Lai Man, Chi</br>
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Characterizing Slow Chemical Exchange in Nucleic Acids by Carbon CEST and Low Spin-Lock Field R1? NMR Spectroscopy
Linear Mode
