Using Chemical Synthesis To Study and Apply Protein Glycosylation
Using Chemical Synthesis To Study and Apply Protein Glycosylation
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Biochemistry
DOI: 10.1021/acs.biochem.7b01055
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nmrlearner
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01-17-2018 05:28 AM
[NMR paper] Palladium in Chemical Protein Synthesis and Modifications
Palladium in Chemical Protein Synthesis and Modifications
The field of site-specific modification of proteins has drawn significant attentions in recent years owing to its high importance in various research areas such as the development of novel therapeutics and understanding the biochemical and cellular behaviors of proteins. The presence of a large number of reactive functional groups in the protein of interest and in the cellular environment renders the particular modification at a specific site a highly challenging task. However, with the development of sophisticated...
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04-07-2017 02:01 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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nmrlearner
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07-16-2016 04:54 AM
[NMR paper] An efficient fusion expression system for protein and peptide overexpression in Esche
An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Related Articles An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Protein Pept Lett. 2003 Apr;10(2):175-81
Authors: Cheng Y, Liu D, Feng Y, Jing G
An efficient fusion expression system with a small fusion partner, His6-tagged N-terminal fragment of staphylococcal nuclease R, has been constructed and tested with two genes. The results show that...
nmrlearner
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11-24-2010 09:01 PM
[NMR paper] A simple efficient synthesis of [23,24]-(13)C(2)-labeled bile salts as NMR probes of
A simple efficient synthesis of -(13)C(2)-labeled bile salts as NMR probes of protein-ligand interactions.
Related Articles A simple efficient synthesis of -(13)C(2)-labeled bile salts as NMR probes of protein-ligand interactions.
Bioorg Med Chem Lett. 2002 Feb 11;12(3):433-5
Authors: Tochtrop GP, DeKoster GT, Cistola DP, Covey DF
The synthesis of -(13)C(2)-labeled bile salts is achieved through a steroidal side chain degradation and isotopic regeneration strategy. Three common bile acids were degraded to the corresponding C(22 )aldehyde by an...
nmrlearner
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11-24-2010 08:49 PM
[NMR paper] Efficient solid-phase synthesis of Vpr from HIV-1 using low quantities of uniformly 1
Efficient solid-phase synthesis of Vpr from HIV-1 using low quantities of uniformly 13C-, 15N-labeled amino acids for NMR structural studies.
Related Articles Efficient solid-phase synthesis of Vpr from HIV-1 using low quantities of uniformly 13C-, 15N-labeled amino acids for NMR structural studies.
J Pept Res. 1999 Nov;54(5):427-35
Authors: Cornille F, Wecker K, Loffet A, Genet R, Roques B
The 96-amino acid protein Vpr functions as a regulator of cellular processes involved in the human immunodeficiency virus, type 1 (HIV-1) life cycle,...
nmrlearner
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11-18-2010 08:31 PM
[NMR paper] Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
Related Articles Efficient enzymatic synthesis of 13C,15N-labeled DNA for NMR studies.
J Biomol NMR. 1997 Oct;10(3):245-53
Authors: Smith DE, Su JY, Jucker FM
The power of heteronuclear NMR spectroscopy to study macromolecules and their complexes has been amply demonstrated over the last decade. The obstacle to routinely applying these techniques to the study of DNA has been the synthesis of 13C,15N-labeled DNA. Here we present a simple and efficient method to generate...
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08-22-2010 05:08 PM
[NMR paper] Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical a
Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Related Articles Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations.
Biochemistry. 1993 Jan 12;32(1):282-9
Authors: Adler M, Carter P, Lazarus RA, Wagner G
The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet...