Related ArticlesCross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes.
J Am Chem Soc. 2003 Aug 27;125(34):10420-8
Authors: Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE
A comparison of HSQC and HMQC pulse schemes for recording (1)H[bond](13)C correlation maps of protonated methyl groups in highly deuterated proteins is presented. It is shown that HMQC correlation maps can be as much as a factor of 3 more sensitive than their HSQC counterparts and that the sensitivity gains result from a TROSY effect that involves cancellation of intra-methyl dipolar relaxation interactions. (1)H[bond](13)C correlation spectra are recorded on U-[(15)N,(2)H], Ile delta 1-[(13)C,(1)H] samples of (i) malate synthase G, a 723 residue protein, at 37 and 5 degrees C, and of (ii) the protease ClpP, comprising 14 identical subunits, each with 193 residues (305 kDa), at 5 degrees C. The high quality of HMQC spectra obtained in short measuring times strongly suggests that methyl groups will be useful probes of structure and dynamics in supramolecular complexes.
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methylâ??methyl nuclear overhauser enhancement spectroscopy
Abstract Methyl-transverse relaxation optimized spectroscopy is rapidly becoming the preferred NMR technique for probing structure and dynamics of very large proteins up to ~1 MDa in molecular size. Data interpretation, however, necessitates assignment of methyl groups which still presents a very challenging and time-consuming process. Here we demonstrate that, in combination with a known 3D structure, paramagnetic...
nmrlearner
Journal club
0
09-26-2011 06:42 AM
NMR Cross-Correlated Relaxation Rates Reveal Ion Coordination Sites in DNA
NMR Cross-Correlated Relaxation Rates Reveal Ion Coordination Sites in DNA
Radovan Fiala, Nad?a S?pac?kova?, Silvie Foldynova?-Tranti?rkova?, Jir?i? S?poner, Vladimi?r Sklena?r? and Luka?s? Tranti?rek
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202397p/aop/images/medium/ja-2011-02397p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202397p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/vJtIag8UbVQ
nmrlearner
Journal club
0
08-13-2011 02:47 AM
How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar Cαâ??Câ?²/HNâ??N cross-correlated relaxation
How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar Cαâ??Câ?²/HNâ??N cross-correlated relaxation
Abstract Highly precise and accurate measurements of very small NMR cross-correlated relaxation rates, namely those between protein HiNâ??Ni and Ciâ??1αâ??Ciâ??1â?² dipoles, are demonstrated with an error of 0.03 sâ??1 for GB3. Because the projection angles between the two dipole vectors are very close to the magic angle the rates range only from â??0.2 to +0.2 sâ??1. Small changes of the average vector orientations have a dramatic impact on the relative values....
nmrlearner
Journal club
0
06-06-2011 12:53 AM
How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar C(?)-C'/H (N)-N cross-correlated relaxation.
How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar C(?)-C'/H (N)-N cross-correlated relaxation.
How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar C(?)-C'/H (N)-N cross-correlated relaxation.
J Biomol NMR. 2011 Jun 3;
Authors: Vögeli B
Highly precise and accurate measurements of very small NMR cross-correlated relaxation rates, namely those between protein H (i) (N) -N(i) and C (i-1) (?) -C(i-1)' dipoles, are demonstrated with an error of 0.03*s(-1) for GB3. Because the projection angles...
nmrlearner
Journal club
0
06-04-2011 11:26 AM
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Abstract Methyl 13CHD2 isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from -glucose/D2O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Alaβ, Thrγ2) is possible using simple â??out-and-backâ?? NMR methodology. Such selective methyl-detected â??out-and-backâ?? NMR experiments allow complete assignments of threonine γ2...
nmrlearner
Journal club
0
01-09-2011 12:46 PM
Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation
Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation
Abstract The measurements of cross-correlated relaxation rates between HNâ??N and Cβâ??Cγ intraresidual and sequential dipolar interactions is demonstrated in ASN, ASP and aromatic residues. The experiment can be used for deuterated samples and no additional knowledge such as Karplus parametrizations is required for the analysis. The data constitutes a new type of information since no other method relates the Cβâ??Cγ bond to HNâ??N. Using this method the dominant populations of rotamer...
nmrlearner
Journal club
0
01-09-2011 12:46 PM
[NMR paper] Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(L
Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
Related Articles Application of cross-correlated NMR spin relaxation to the zinc-finger protein CRP2(LIM2): evidence for collective motions in LIM domains.
Biochemistry. 2001 Aug 14;40(32):9596-604
Authors: Schüler W, Kloiber K, Matt T, Bister K, Konrat R
The solution structure of quail CRP2(LIM2) was significantly improved by using an increased number of NOE constraints obtained from a 13C,15N-labeled...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Polarization transfer by cross-correlated relaxation in solution NMR with very large
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4918-23
Authors: Riek R, Wider G, Pervushin K, Wüthrich...
![Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in](http://www.bionmr.com/forum/iconimages/journal-club-9/cross-correlated-relaxation-enhanced-1h%5Bbond%5D13c-nmr-spectroscopy-methyl-groups_ltr.gif)
Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in
Linear Mode
