Related ArticlesDetermining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Chem Commun (Camb). 2017 Aug 25;:
Authors: Gerecht K, Figueiredo AM, Hansen DF
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of arginine side chains. An application to a 19 kDa protein shows that the strengths of interactions involving arginine side chains can be characterised.
PMID: 28840203 [PubMed - as supplied by publisher]
[NMR paper] Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.
Angew Chem Int Ed Engl. 2013 Mar 11;52(11):3145-7
Authors: Werbeck ND, Kirkpatrick J,...
[NMR paper] NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins.
Adv Protein Chem Struct Biol. 2013;93:37-80
Authors: Zandarashvili L, Esadze A, Iwahara J
Abstract
Hydrogen bonds and ion pairs involving side chains play vital roles in protein functions such as...
[NMR paper] Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N r
Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
Related Articles Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2001 Feb 7;123(5):967-75
Authors: Mulder FA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE
A new NMR experiment is presented for...
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[NMR paper] Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fra
Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments.
Related Articles Carbon-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...
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
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