Related ArticlesAnalysis of protein-carbohydrate interaction at the lower size limit of the protein part (15-mer peptide) by NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling.
Biochemistry. 2002 Jul 30;41(30):9707-17
Authors: Siebert HC, Lü SY, Frank M, Kramer J, Wechselberger R, Joosten J, André S, Rittenhouse-Olson K, Roy R, von der Lieth CW, Kaptein R, Vliegenthart JF, Heck AJ, Gabius HJ
Structural analysis of minimally sized lectins will offer insights into fundamentals of intermolecular recognition and potential for biomedical applications. We thus moved significantly beyond the natural limit of lectin size to determine the structure of synthetic mini-lectins in solution, their carbohydrate selectivity and the impact of ligand binding on their conformational behavior. Using three disaccharide (Thomsen-Friedenreich antigen; Gal beta 1,3GalNAc alpha 1,R)-binding pentadecapeptides without internal disulfide bridges as role models, we successfully tested a combined strategy with different techniques of NMR spectroscopy, electrospray ionization mass spectrometry, and molecular modeling. In solution, the peptides invariably displayed flexibility with rather limited restrictions, shown by NMR experiments including nearly complete resonance assignments and molecular dynamics simulations. The occurrence of aromatic/nonpolar amino acids in the sequence did not lead to formation of a hydrophobic core known from microbial chitinase modules. Selectivity of disaccharide binding was independently observed by mass spectrometry and NMR analysis. Specific ligand interaction yielded characteristic NMR signal alterations but failed to reduce conformational flexibility significantly. We have thereby proven effectiveness of our approach to analyze even low-affinity interactions (not restricted to carbohydrates as ligands). It will be useful to evaluate the impact of rational manipulation of lead peptide sequences.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid ?-protein fibrils.
Bioorg Med Chem. 2011 Aug 27;
Authors: Masuda Y, Fukuchi M, Yatagawa T, Tada M, Takeda K, Irie K, Akagi KI, Monobe Y, Imazawa T, Takegoshi K
Abstract
Aggregation of 42-residue amyloid ?-protein (A?42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts...
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09-20-2011 03:10 PM
Carbohydrate-Protein Interactions: A 3D View by NMR.
Carbohydrate-Protein Interactions: A 3D View by NMR.
Carbohydrate-Protein Interactions: A 3D View by NMR.
Chembiochem. 2011 Apr 15;
Authors: Roldós V, Cañada FJ, Jiménez-Barbero J
This review focuses on the application of NMR methods for understanding, at the molecular and atomic levels, the diverse mechanisms by which sugar molecules are recognised by the binding sites of lectins, antibodies and enzymes. Given the intrinsic chemical natures of sugars and their flexibility, it is well established that NMR parameters should be complemented by...
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04-19-2011 11:01 PM
[NMR paper] NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-
NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions.
Related Articles NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions.
Carbohydr Res. 2004 Apr 2;339(5):907-28
Authors: Johnson MA, Pinto BM
Investigations of the conformations of carbohydrates, their analogues and their molecular mimics are described, with emphasis on structural and functional information that can be gained by NMR spectroscopic techniques in combination with molecular...
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11-24-2010 09:51 PM
[NMR paper] Detection of the protein-protein interaction between cyclic AMP receptor protein and
Detection of the protein-protein interaction between cyclic AMP receptor protein and RNA polymerase, by (13)C-carbonyl NMR.
Related Articles Detection of the protein-protein interaction between cyclic AMP receptor protein and RNA polymerase, by (13)C-carbonyl NMR.
J Biochem. 2001 Jul;130(1):57-61
Authors: Lee TW, Won HS, Park SH, Kyogoku Y, Lee BJ
Cyclic AMP receptor protein (CRP) plays a key role in the transcription regulation of many prokaryotic genes. Upon the binding of cyclic AMP, CRP is allosterically activated, binds to target DNA...
Analysis of protein-carbohydrate interaction at the lower size limit of the protein p
Linear Mode
