Related ArticlesPurification of cloned trypanosomal calmodulin and preliminary NMR studies.
J Chromatogr. 1991 Feb 22;539(2):501-5
Authors: Sweeney PJ, Walker JM, Reid DG, Elshourbagy N
Cloned trypanosomal calmodulin was expressed in Escherichia coli and purified to homogeneity using hydrophobic interaction chromatography on phenyl-Sepharose. The purified protein was subjected to NMR analysis which allows detailed changes to be observed when, firstly, calcium, and secondly, the drug calmidazolium bind. These spectral changes are the result of conformational changes in the protein and proximity effects due to the drug.
[NMR paper] Expression, purification, crystallization, and NMR studies of the helicase interactio
Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.
Related Articles Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase.
Protein Expr Purif. 2004 Feb;33(2):304-10
Authors: Loscha K, Oakley AJ, Bancia B, Schaeffer PM, Prosselkov P, Otting G, Wilce MC, Dixon NE
In Escherichia coli, the DnaG primase is the RNA polymerase that synthesizes RNA primers at replication forks. It is composed of three...
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[NMR paper] Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the e
Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
Related Articles Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
J Struct Biol. 2000 Aug;131(2):164-9
Authors: Hamdan S, Brown SE, Thompson PR, Yang JY, Carr PD, Ollis DL, Otting G, Dixon NE
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA...
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[NMR paper] Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in
Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
FEBS Lett. 1997 Sep 29;415(2):155-9
Authors: Davydova NL, Rak AV, Gryaznova OI, Liljas A, Jonsson BH, Berglund H, Härd T, Garber MB
The gene for the ribosomal protein S19 from Thermus thermophilus was cloned,...
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[NMR paper] Cloning, purification, and preliminary characterization by circular dichroism and NMR
Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22...
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[NMR paper] Cloning, purification, and preliminary characterization by circular dichroism and NMR
Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22...
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[NMR paper] NMR studies of caldesmon-calmodulin interactions.
NMR studies of caldesmon-calmodulin interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of caldesmon-calmodulin interactions.
Biochemistry. 1997 Mar 11;36(10):2817-25
Authors: Zhou N, Yuan T, Mak AS, Vogel HJ
The binding of the calcium-regulatory protein calmodulin (CaM) to caldesmon (CaD) contributes to the regulation of smooth muscle contraction. Two regions of caldesmon have been identified as putative calmodulin-binding domains. We have earlier reported on the...
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[NMR paper] Protein engineering and NMR studies of calmodulin.
Protein engineering and NMR studies of calmodulin.
Related Articles Protein engineering and NMR studies of calmodulin.
Mol Cell Biochem. 1995 Aug-Sep;149-150:3-15
Authors: Vogel HJ, Zhang M
The calcium regulatory protein calmodulin (CaM) plays a role as an on-off switch in the activation of many enzymes and proteins. CaM has a dumbbell shaped structure with two folded domains, which are connected by a flexible linker in solution. The calmodulin-binding domains of the target proteins are contained in 20 residue long amino acid sequences, that...
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[NMR paper] 1H NMR studies on bovine cyclophilin: preliminary structural characterization of its
1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
Related Articles 1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
Biochemistry. 1990 May 8;29(18):4466-78
Authors: Heald SL, Harding MW, Handschumacher RE, Armitage IM
Cyclophilin (163 residues, Mr 17737), a peptidyl prolyl cis-trans isomerase, is a cytosolic protein that specifically binds the potent immunosuppressant cyclosporin A (CsA). The native form of the major...