Related ArticlesNMR studies on the flexibility of nucleoside diphosphate kinase.
Proteins. 1997 Jun;28(2):150-2
Authors: Xu Y, Lecroisey A, Veron M, Delepierre M, Janin J
Human NDP kinase B, product of the nm23-H2 gene, binds DNA. It has been suggested that a helix hairpin on the protein surface, part of the nucleotide substrate binding site, could accommodate DNA binding by swinging away. The presence of flexible regions was therefore investigated by 1H NMR dynamic filtering. Although TOCSY peaks could be assigned to five residues at the N terminus of Dictyostelium NDP kinase, no flexible region was detected in the human enzyme. These data favor the idea that the protein offers different binding sites to mono- and polynucleotides.
[NMR paper] NMR studies of the backbone flexibility and structure of human growth hormone: a comp
NMR studies of the backbone flexibility and structure of human growth hormone: a comparison of high and low pH conformations.
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J Mol Biol. 2002 May 3;318(3):679-95
Authors: Kasimova MR, Kristensen SM, Howe PW, Christensen T, Matthiesen F, Petersen J, Sørensen HH, Led JJ
(15)N NMR relaxation parameters and amide (1)H/(2)H-exchange rates have been used to characterize the structural flexibility of human...
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[NMR paper] Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (3
Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.
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Biochemistry. 2002 May 14;41(19):5968-77
Authors: Seifert MH, Breitenlechner CB, Bossemeyer D, Huber R, Holak TA, Engh RA
Cell signaling pathways rely on phosphotransfer reactions that are catalyzed by protein kinases. The protein kinases themselves are typically regulated by phosphorylation and concurrent structural...
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[NMR paper] A novel view of domain flexibility in E. coli adenylate kinase based on structural mo
A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
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J Mol Biol. 2002 Jan 11;315(2):155-70
Authors: Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E
Adenylate kinase from Escherichia coli (AKeco), consisting of a single 23.6 kDa polypeptide chain folded into domains CORE, AMPbd and LID, catalyzes the reaction AMP+ATP-->2ADP. In the...
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[NMR paper] NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff
NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.
J Biol Chem. 1997 Jan 3;272(1):362-8
Authors: Lecroisey A, Martineau P, Hofnung M, Delepierre M
A set of permissive positions that tolerate...
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[NMR paper] NMR studies on the flexibility of nucleoside diphosphate kinase.
NMR studies on the flexibility of nucleoside diphosphate kinase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR studies on the flexibility of nucleoside diphosphate kinase.
Proteins. 1997 Jun;28(2):150-2
Authors: Xu Y, Lecroisey A, Veron M, Delepierre M, Janin J
Human NDP kinase B, product of the nm23-H2 gene, binds DNA. It has been suggested that a helix hairpin on the protein surface, part of the nucleotide substrate binding...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff
NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.
J Biol Chem. 1997 Jan 3;272(1):362-8
Authors: Lecroisey A, Martineau P, Hofnung M, Delepierre M
A set of permissive positions that tolerate...
[NMR paper] Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dC
Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dCDP is a competitive inhibitor and functions as a spectroscopic probe for the substrate binding site; demonstration by enzyme kinetics and 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dCDP is a competitive inhibitor and functions as a spectroscopic probe for the substrate binding site;...
NMR studies on the flexibility of nucleoside diphosphate kinase.
Linear Mode
