Reducing sugars can spontaneously react with free amines in protein side chains leading to posttranslational modifications (PTMs) called glycation. In contrast to glycosylation, glycation is a non-enzymatic modification with consequences on the overall charge, solubility, aggregation susceptibility and functionality of a protein. Glycation is a critical quality attribute of therapeutic monoclonal antibodies. In addition to glucose, also disaccharides like maltose can form glycation products. We...
The NMR signature of maltose-based glycation in full-length proteins
The NMR signature of maltose-based glycation in full-length proteins
Abstract
Reducing sugars can spontaneously react with free amines in protein side chains leading to posttranslational modifications (PTMs) called glycation. In contrast to glycosylation, glycation is a non-enzymatic modification with consequences on the overall charge, solubility, aggregation susceptibility and functionality of a protein. Glycation is a critical quality attribute of therapeutic monoclonal antibodies. In addition to glucose, also disaccharides like maltose can form...
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12-21-2023 03:08 PM
[NMR paper] NMR structure of a full-length single-pass membrane protein NRADD.
NMR structure of a full-length single-pass membrane protein NRADD.
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Proteins. 2019 Apr 29;:
Authors: Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS
Abstract
Structural study of any single-pass membrane protein is both an important and challenging task. In this report, we present the structure of a neurotrophin receptor-alike death-domain protein, NRADD. The structure and dynamics of the protein was investigated by conventional nuclear magnetic...
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04-30-2019 03:58 PM
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
A Novel Domain Assembly Routine for Creating Full-Length Models of Membrane Proteins from Known Domain Structures
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00995/20171211/images/medium/bi-2017-00995a_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00995
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/IYVe61xDFY0
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12-12-2017 02:12 AM
[NMR paper] A new glycation product 'norpronyl-lysine,' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
A new glycation product 'norpronyl-lysine,' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Related Articles A new glycation product 'norpronyl-lysine,' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Biosci Rep. 2014 Apr 01;34(2):
Authors: Bullock PT, Reid DG, Ying Chow W, Lau WP, Duer MJ
Abstract
NMR is ideal for characterizing non-enzymatic protein glycation, including AGEs (advanced glycation...
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12-07-2016 01:26 PM
[NMR paper] A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Related Articles A new glycation product 'norpronyl-lysine' and direct characterization of cross linking and other glycation adducts: NMR of model compounds and collagen.
Biosci Rep. 2014 Feb 12;
Authors: Bullock PT, Reid DG, Chow WY, Lau WP, Duer MJ
Abstract
NMR is ideal for characterizing non-enzymatic protein glycation, including AGEs (advanced glycation end products) underlying...
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02-13-2014 03:35 PM
[NMR paper] Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscop
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
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J Biomed Sci. 2005;12(3):451-6
Authors: Briese L, Preusser A, Willbold D
The Nef protein of human immunodeficiency virus type 1 (HIV-1) is known to directly bind to the SH3 domain of human lymphocyte specific kinase (Lck) via a proline-rich region located in the amino terminal part of Nef. To address the question whether Nef binding to Lck SH3 involves...
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11-24-2010 11:14 PM
[NMR paper] Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepar
Functional characterization and NMR spectroscopy on full-length Vpu from HIV-1 prepared by total chemical synthesis.
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J Am Chem Soc. 2004 Mar 3;126(8):2439-46
Authors: Kochendoerfer GG, Jones DH, Lee S, Oblatt-Montal M, Opella SJ, Montal M
Vpu is an 81-residue integral membrane protein encoded in the HIV-1 genome that is of considerable interest because it plays important roles in the release of virus particles...
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11-24-2010 09:25 PM
[NMR paper] NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima.
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J Biomol NMR. 2003 Feb;25(2):163-4
Authors: Ilin S, Hoskins A, Schwalbe H, Wöhnert J
The NMR signature of maltose-based glycation in full-length proteins
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