[NMR images] Nucleic acid and protein NMR
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Nucleic acid and protein NMR
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11-12-2011 01:40 AM
Optimization of amino acid type-specific (13)C and (15)N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm.
Optimization of amino acid type-specific (13)C and (15)N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm.
Optimization of amino acid type-specific (13)C and (15)N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm.
J Biomol NMR. 2010 Dec 18;
Authors: Hefke F, Bagaria A, Reckel S, Ullrich SJ, Dötsch V, Glaubitz C, Güntert P
We present a computational method for finding optimal labeling patterns for the backbone...
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12-21-2010 01:00 PM
Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm
Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm
Abstract We present a computational method for finding optimal labeling patterns for the backbone assignment of membrane proteins and other large proteins that cannot be assigned by conventional strategies. Following the approach of Kainosho and Tsuji (Biochemistry 21:6273â??6279 (1982)), types of amino acids are labeled with 13C or/and 15N such that cross peaks between 13CO(i â?? 1) and 15NH(i) result only for pairs...
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12-21-2010 02:14 AM
[NMR paper] NMR studies of protein-nucleic acid interactions.
NMR studies of protein-nucleic acid interactions.
Related Articles NMR studies of protein-nucleic acid interactions.
Methods Mol Biol. 2004;278:289-312
Authors: Varani G, Chen Y, Leeper TC
Protein-DNA and protein-RNA complexes play key functional roles in every living organism. Therefore, the elucidation of their structure and dynamics is an important goal of structural and molecular biology. Nuclear magnetic resonance (NMR) studies of protein and nucleic acid complexes have common features with studies of protein-protein complexes: the...
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11-24-2010 09:25 PM
[NMR paper] Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and ir
Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
Related Articles Amino acid-specific isotopic labeling and active site NMR studies of iron(II)- and iron(III)-superoxide dismutase from Escherichia coli.
J Biomol NMR. 2000 Aug;17(4):311-22
Authors: Sorkin DL, Miller AF
We have developed and employed multiple amino acid-specific isotopic labeling schemes to obtain definitive assignments for active site 1H NMR resonances of iron(II)- and iron(III)-superoxide...
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11-19-2010 08:29 PM
[NMR paper] Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of
Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Labeling of recombinant protein for NMR spectroscopy: global and specific labeling of the rat liver fructose 2,6-bisphosphatase domain.
Protein Expr Purif. 1997 Oct;11(1):79-85
Authors: Okar DA, Felicia ND, Gui L, Lange AJ
Methods for the efficient use of the 13C-labeled nutrients,...
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08-22-2010 05:08 PM
[NMR paper] NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and co
NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Related Articles NMR studies of protein-nucleic acid complexes: structures, solvation, dynamics and coupled protein folding.
Q Rev Biophys. 1999 Feb;32(1):57-98
Authors: Härd T
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08-21-2010 04:03 PM
[NMR paper] Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled ba
Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: potential for NMR structure determination of large proteins.
Related Articles Application of amino acid type-specific 1H- and 14N-labeling in a 2H-, 15N-labeled background to a 47 kDa homodimer: potential for NMR structure determination of large proteins.
J Biomol NMR. 1999 May;14(1):79-83
Authors: Kelly MJ, Krieger C, Ball LJ, Yu Y, Richter G, Schmieder P, Bacher A, Oschkinat H
NMR investigations of larger macromolecules (> 20...
Specific Labeling of ThreonineMethyl Groups for NMR Studies of Protein–Nucleic Acid Complexes
Linear Mode
