[NMR paper] Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics...
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08-31-2016 02:34 PM
Photooxidation of Tryptophan and Tyrosine Residuesin Human Serum Albumin Sensitized by Pterin: A Model for GlobularProtein Photodamage in Skin
Photooxidation of Tryptophan and Tyrosine Residuesin Human Serum Albumin Sensitized by Pterin: A Model for GlobularProtein Photodamage in Skin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00420/20160817/images/medium/bi-2016-004204_0013.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00420
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08-19-2016 04:05 AM
Synthesis and Kinetic Analysis of Two ConformationallyRestricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5
Synthesis and Kinetic Analysis of Two ConformationallyRestricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00576/20160715/images/medium/bi-2016-00576v_0011.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00576
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07-16-2016 04:54 AM
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00995/20151215/images/medium/bi-2015-00995k_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00995
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[U. of Ottawa NMR Facility Blog] Dead Time and Phase
Dead Time and Phase
The phase of an NMR peak depends on the sine/cosine character of the free induction decay (FID) when the receiver is turned on. Positive and negative cosine FIDs will yield positive and negative in-phase peaks, respectively whereas positive or negative sine FIDs will yield peaks 90° out of phase. FIDs that are neither a pure sine nor pure cosine with yield peaks which are out of phase to an extent dependent on the cosine/sine character of the FID. In a perfect world, the receiver is gated on immediately after a perfect 90° pulse and all FID’s are cosines producing...
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04-29-2015 03:14 AM
[NMR paper] NMR assignment of the gpU tail protein from lambda bacteriophage.
NMR assignment of the gpU tail protein from lambda bacteriophage.
Related Articles NMR assignment of the gpU tail protein from lambda bacteriophage.
J Biomol NMR. 2005 May;32(1):91-2
Authors: Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L
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11-25-2010 08:21 PM
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
Related Articles Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
The DEAD-Box Protein CYT-19 Uses Arginine Residuesin Its C-Tail To Tether RNA Substrates
Linear Mode
