Related ArticlesCarbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments.
J Protein Chem. 1993 Dec;12(6):695-707
Authors: Huque ME, Vogel HJ
The pH-titration and dynamic behaviour of the seven lysine side chains in bovine calmodulin were studied by carbon-13 NMR. The amino groups of the calcium saturated protein and its proteolytic fragments TR1C (1-75) and TR2C (78-148) were dimethylated with carbon-13 labeled formaldehyde; this modification did not alter the protein's structure or its ability to activate the enzyme cyclic nucleotide phosphodiesterase. Tentative assignments for 5 out of the 7 dimethyl lysine resonances could be obtained by comparing spectra of the fully and partially modified protein, with those of the proteolytic fragments. The pKa values measured for calcium saturated calmodulin ranged between 9.5 (Lys 75) and 10.2 (Lys 13); two residues (Lys 94 and Lys 13) showed a biphasic titration curve suggesting their possible involvement in ion-pairs. The dynamic behavior of the lysine side chains was deduced from spin lattice relaxation measurements. All side chains were flexible and this was not influenced by the removal of calcium, or the addition of the calmodulin antagonist trifluoperazine. The latter data suggest that the lysine side chains are not directly involved in calmodulin's target binding sites.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
J Biomol NMR. 2011 Sep 25;
Authors: Huang W, Varani G, Drobny GP
Abstract
Formation of the complex between human immunodeficiency virus type-1 Tat protein and the transactivation response region (TAR) RNA is vital for transcriptional elongation, yet the structure of the Tat-TAR complex remains to be established. The NMR structures of free TAR, and TAR bound to Tat-derived...
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09-30-2011 06:00 AM
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
Interactions of protein side chains with RNA defined with REDOR solid state NMR.
J Biomol NMR. 2011 Sep 25;
Authors: Huang W, Varani G, Drobny GP
Abstract
Formation of the complex between human immunodeficiency virus type-1 Tat protein and the transactivation response region (TAR) RNA is vital for transcriptional elongation, yet the structure of the Tat-TAR complex remains to be established. The NMR structures of free TAR, and TAR bound to Tat-derived...
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09-30-2011 05:59 AM
[CNS Yahoo group] Double protonated His side chains have charge +1 independent of pH
Double protonated His side chains have charge +1 independent of pH
Hi all, I am using ccpn/aria/cns combination for my structural work. I discovered a probably bad fact during the aria/cns structure calculation. In the ccpn
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01-20-2011 03:28 AM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iFwgRBt-zto
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12-28-2010 05:27 AM
[NMR paper] The effects of mutations on motions of side-chains in protein L studied by 2H NMR dyn
The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.
Related Articles The effects of mutations on motions of side-chains in protein L studied by 2H NMR dynamics and scalar couplings.
J Mol Biol. 2003 Jun 6;329(3):551-63
Authors: Millet O, Mittermaier A, Baker D, Kay LE
Recently developed 2H spin relaxation experiments are applied to study the dynamics of methyl-containing side-chains in the B1 domain of protein L and in a pair of point mutants of the domain, F22L and A20V. X-ray and...
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11-24-2010 09:01 PM
[NMR paper] Determination of pKa values of the histidine side chains of phosphatidylinositol-spec
Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus by NMR spectroscopy and site-directed mutagenesis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Determination of pKa values of the histidine side chains of phosphatidylinositol-specific phospholipase C from Bacillus cereus...
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08-22-2010 05:08 PM
[NMR paper] Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide
Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study.
J Biol Chem. 1999 Mar 26;274(13):8411-20
Authors: Yuan T, Ouyang H, Vogel HJ
Binding of calcium to calmodulin (CaM) causes a conformational...