Related ArticlesObservation of a new nonfluorescent malondialdehyde-acetaldehyde-protein adduct by 13C NMR spectroscopy.
Chem Res Toxicol. 1999 Jan;12(1):100-5
Authors: Kearley ML, Patel A, Chien J, Tuma DJ
It has been shown that malondialdehyde (MDA) and acetaldehyde react with proteins via the epsilon-amino group of a lysine residue to yield hybrid MDA-acetaldehyde (MAA)-protein adducts. The structure of one MAA adduct has been confirmed to be 4-methyl-1, 4-dihydropyridine-3,5-dicarbaldehyde (3). In this study, 13C NMR spectroscopy was used to identify the structure of a second MAA adduct as 2-formyl-3-(alkylamino)butanal (4). Isotopically labeled [1-13C]acetaldehyde was reacted with MDA and the protein, bovine serum albumin, under a variety of conditions, and the reactions were monitored at various time intervals by 13C NMR. In each experiment, new signals grew in at 50 and 22 ppm. By comparison to model compounds, the signals at 50 ppm correspond to a 2-formyl-3-(alkylamino)butanal adduct and the signals at 22 ppm correspond to the known 1,4-dihydropyridine-3,5-dicarbaldehyde adduct. Similar results were found when the BSA was replaced with polylysine. Overall, it appears that MAA-protein adducts are composed of two major products, 3 and 4.
[NMR paper] Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Related Articles Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12748-53
Authors: Horst R, Bertelsen EB, Fiaux J, Wider G, Horwich AL, Wüthrich K
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the...
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[NMR paper] Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid s
Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
Related Articles Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
J Mol Biol. 2002 Nov 8;323(5):899-907
Authors: Stumber M, Geyer M, Graf R, Kalbitzer HR, Scheffzek K, Haeberlen U
The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein...
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[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
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[NMR paper] NMR observation of selected segments in a larger protein: central-segment isotope lab
NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Related Articles NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Biochemistry. 1999 Dec 7;38(49):16040-4
Authors: Otomo T, Ito N, Kyogoku Y, Yamazaki T
Peptide segments in a protein, which can include an active site of interest or be a series of parts constituting the entire structure, are now selectively observed by nuclear magnetic resonance...
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[NMR paper] Observation of reorientationally hindered water in biological tissue using triple qua
Observation of reorientationally hindered water in biological tissue using triple quantum filtered 17O-NMR.
Related Articles Observation of reorientationally hindered water in biological tissue using triple quantum filtered 17O-NMR.
Biochim Biophys Acta. 1995 Jun 9;1244(2-3):253-8
Authors: Flesche CW, Gruwel ML, Deussen A, Schrader J
Water dynamics in aqueous biopolymer solutions often display a two-phase character, resembling water-water and water-protein interactions. Rotationally hindered water molecules in crowded protein environments...
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[NMR paper] Characterization by NMR of the heme-myoglobin adduct formed during the reductive meta
Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group.
Related Articles Characterization by NMR of the heme-myoglobin adduct formed during the reductive metabolism of BrCCl3. Covalent bonding of the proximal histidine to the ring I vinyl group.
J Biol Chem. 1991 Feb 15;266(5):3208-14
Authors: Osawa Y, Highet RJ, Bax A, Pohl LR
The reductive debromination of BrCCl3 by ferrous deoxymyoglobin leads to the covalent bonding of the...
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[NMR paper] Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of p
Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions.
J Magn Reson. 1999 Feb;136(2):214-8
Authors: Melacini G, Kaptein R, Boelens R
An experimental approach for the editing of exchange-relayed NOEs in water-selective NOE experiments is presented. The...