This is CspA with eight surface aromatic side chains visible:
11/06/2014 6:46:13 AM GMT
This is CspA with eight surface aromatic side chains visible: More...
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[NMR paper] Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
J Biomol NMR. 2014 Jan 4;
Authors: Kovacs H, Gossert A
Abstract
Three improved (13)C-spinlock experiments for side chain assignments of...
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01-07-2014 11:16 PM
[KPWU blog] [PyMOL] side-by-side comparison of 3 electrostatic surface potentials
side-by-side comparison of 3 electrostatic surface potentials
Here is an example using “grid mode” provided in PyMOL to show the charged states of a protein (PDB entry: 1Z66) at pH 4 (left), 7 (center) and 11 (right). *PyMOL script is attached after the figure. First, *the potential maps at three pH states have to be generated. I used APBS web http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=798&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
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09-18-2012 02:58 PM
Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion
Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected 13C CPMG relaxation dispersion
Abstract Protein dynamics on the millisecond time scale commonly reflect conformational transitions between distinct functional states. NMR relaxation dispersion experiments have provided important insights into biologically relevant dynamics with site-specific resolution, primarily targeting the protein backbone and methyl-bearing side chains. Aromatic side chains represent attractive probes of protein dynamics because they are over-represented in protein binding...
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07-30-2012 07:42 AM
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
13C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
Abstract Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics of aromatic side chains and its response to biologically relevant events. Indeed, measurements of 13C relaxation rates in aromatic moieties have a long history in biomolecular NMR, primarily in the context of...
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07-05-2012 04:13 AM
[Question from NMRWiki Q&A forum] selecting for side chains
selecting for side chains
Does anyone know of literature pointing to NMR experiments that can select for say -CH3 groups attached to -CH2?
Check if somebody has answered this question on NMRWiki QA forum
nmrlearner
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06-05-2012 05:58 PM
4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins
4D APSY-HBCB(CG)CDHD experiment for automated assignment of aromatic amino acid side chains in proteins
Abstract A four-dimensional (4D) APSY (automated projection spectroscopy)-HBCB(CG)CDHD experiment is presented. This 4D experiment correlates aromatic with aliphatic carbon and proton resonances from the same amino acid side chain of proteins in aqueous solution. It thus allows unambiguous sequence-specific assignment of aromatic amino acid ring signals based on backbone assignments. Compared to conventional 2D approaches, the inclusion of evolution periods on 1Hβ and 13Cδ...
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09-30-2011 08:01 PM
[NMRwiki tweet] nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.n
nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.nmrwiki.org/question/199/
nmrwiki: Why HCCH TOCSY does not work for whole aromatic side chains? #nmrhttp://qa.nmrwiki.org/question/199/
Source: NMRWiki tweets
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11-18-2010 06:16 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...