Nature methods (2011). Volume: 8, Issue: 11. Pages: 919-31. Jameson R Bothe, Evgenia N Nikolova, Catherine D Eichhorn, Jeetender Chugh, Alexandar L Hansen, Hashim M Al-Hashimi et al.
Many recently discovered noncoding RNAs do not fold into a single native conformation but sample many different conformations along their free-energy landscape to carry out their biological function. Here we review solution-state NMR techniques that measure the structural, kinetic and thermodynamic characteristics of RNA motions spanning picosecond to second timescales at atomic resolution, allowing unprecedented insights into the RNA dynamic structure landscape. From these studies a basic description of the RNA dynamic structure landscape is emerging, bringing new insights into how RNA structures change to carry out their function as well as applications in RNA-targeted drug discovery and RNA bioengineering.
[NMR Sparky Yahoo group] Re: cyana
Re: cyana
Replace all M with Q using any text editor. That should take care of this except if you have pseudo atom names for carbon like CQD etc. In that event change
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nmrlearner
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10-15-2012 10:49 PM
[NMR Sparky Yahoo group] Re: cyana
Re: cyana
Hi, Cyana will not accept Q in carbon atom names. You need to explicitly call it CD1 and CD2 etc. (Please see the link sent by Eiso). Please also see what I
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3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample
Abstract The feasibility of practically complete backbone and ILV methyl chemical shift assignments from a single -labeled protein sample of the truncated form of ligand-free Bst-Tyrosyl tRNA Synthetase (Bst-Î?YRS), a 319-residue predominantly helical homodimer, is established. Protonation of ILV residues at methyl positions does not appreciably detract from the quality of TROSY triple resonance data. The assignments are performed at 40 °C to improve the sensitivity of...
nmrlearner
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09-10-2012 01:48 AM
[Question from NMRWiki Q&A forum] How to extract inter distance restraints of homodimer protein from known crystal structure ?
How to extract inter distance restraints of homodimer protein from known crystal structure ?
Hello friends ,
my target protein exist as dimer and tetrameter , I would like to calculate the solution structure of dimer . i want extract inter distance restraints between two monomers of homo-dimer protein by using known crystal structure( pdb ). Unfortunately my c13 and n15 filter noesy experiment is failed . How to extract distance restraints from pdb of Homodimer .
Regards Srinivas
nmrlearner
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04-13-2012 08:21 PM
[Question from NMRWiki Q&A forum] c13 filter noesy experment for homodimer protein
c13 filter noesy experment for homodimer protein
Dear wikiers
I would like to take c13 filter noesy experment for homodimer protein , total 20 kd size . could you please suggest which parameters should i consider more specificly while taking this experment to get best signal because i dont want to try on trial and error method. any knid of help is greatly appreciated
Thanking you in advance
Regards sri
nmrlearner
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06-30-2011 05:06 PM
Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
Related Articles Combining NMR and EPR Methods for Homodimer Protein Structure Determination.
J Am Chem Soc. 2010 Aug 10;
Authors: Yang Y, Ramelot TA, McCarrick RM, Ni S, Feldmann EA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using...
nmrlearner
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08-17-2010 03:36 AM
Combining NMR and EPR Methods for Homodimer Protein Structure Determination
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja105080h/aop/images/medium/ja-2010-05080h_0003.gif
Combining NMR and EPR Methods for Homodimer Protein Structure Determination
There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis on integrating distinct and complementary methodologies for structure determination of multiprotein ...