Investigation of solvent effect and NMR shielding tensors of p53 tumor-suppressor gene in drug design.
Int J Nanomedicine. 2011;6:213-8
Authors: Irani S, Monajjemi M, Honarparvar B, Atyabi S, Sadeghizadeh M
Abstract
The p53 tumor-suppressor gene encodes a nuclear phosphoprotein with cancer- inhibiting properties. The most probable cancerous mutations occur as point mutations in exons 5 up to 8 of p53, as a base pair substitution that encompasses CUA and GAT sequences. As DNA drug design represents a direct genetic treatment of cancer, in the research reported computational drug design was carried out to explore, at the Hartree-Fock level, effects of solvents on the thermochemical properties and nuclear magnetic resonance (NMR) shielding tensors of some atoms of CUA involved in the hydrogen-bonding network. The observed NMR shielding variations of the solutes caused by solvent change seemed significant and were attributed to solvent polarity, and solute-solvent and solvent-solute hydrogen-bonding interactions. The results provide a reliable insight into the nature of mutation processes. However, to improve our knowledge of the hydration pattern more rigorous computations of the hydrated complexes are needed.
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net
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Biochemists reveal interaction between tumor suppressor protein and chaperone
News-Medical.net
Using nuclear magnetic resonance (NMR) spectroscopy, the scientists at the Bavarian NMR Center in Garching were able for the first time to characterize the interaction surfaces between Hsp90 and p53 and show that p53 binds to Hsp90 in an already ...
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09-08-2011 08:24 AM
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Abstract We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3....
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02-11-2011 08:36 PM
[NMR paper] The (17)O-NMR shielding range and shielding time scale and detection of discrete hydr
The (17)O-NMR shielding range and shielding time scale and detection of discrete hydrogen-bonded conformational states in peptides.
Related Articles The (17)O-NMR shielding range and shielding time scale and detection of discrete hydrogen-bonded conformational states in peptides.
Biopolymers. 2001 Sep;59(3):125-30
Authors: Gerothanassis IP
The (17)O-NMR shielding range and shielding time scale due to hydrogen-bonding interactions in peptides are critically evaluated relative to those of (1)H-NMR. Furthermore, the assumptions and conclusions in...
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11-19-2010 08:44 PM
[NMR paper] Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B
Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data.
Related Articles Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data.
Protein Sci. 2000 Jun;9(6):1120-8
Authors: Yuan C, Selby TL, Li J, Byeon IJ, Tsai MD
Within the tumor suppressor protein INK4 (inhibitor of cyclin-dependent kinase 4) family, p15INK4B is the smallest and the only one whose structure has not been determined...
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11-18-2010 09:15 PM
Oligo design tools for gene synthesis
Oligo design tools for gene synthesis
1 DNAWorks: http://helixweb.nih.gov/dnaworks/
2 TmPrime: http://prime.ibn.a-star.edu.sg/
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Proteins
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08-25-2010 04:37 AM
[NMR paper] Tumor suppressor p16INK4A: structural characterization of wild-type and mutant protei
Tumor suppressor p16INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Tumor suppressor p16INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism.
Biochemistry. 1996 Jul 23;35(29):9475-87
Authors: Tevelev A, Byeon IJ, Selby T, Ericson K, Kim HJ, Kraynov V, Tsai MD
The tumor suppressor p16INK4A with eight N-terminal amino acids deleted (p16/delta 1-8)...
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08-22-2010 02:20 PM
[NMR paper] NMR spectroscopy in structure-based drug design.
NMR spectroscopy in structure-based drug design.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR spectroscopy in structure-based drug design.
Curr Opin Biotechnol. 1999 Feb;10(1):42-7
Authors: Roberts GC
NMR methods for the study of motion in proteins continue to improve, and a number of studies of protein-ligand complexes relevant to drug design have been reported over the past year, for example, studies of fatty-acid-binding protein and SH2 and SH3 domains. These...
Investigation of solvent effect and NMR shielding tensors of p53 tumor-suppressor gene in drug design.
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