Related ArticlesDynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex.
J Mol Biol. 1999 Jun 18;289(4):683-90
Authors: Jin C, Marsden I, Chen X, Liao X
Genesis is an HNF-3/fkh homologous protein. By using multi-dimensional NMR techniques, we have obtained the solution structure and backbone dynamics of Genesis complexed with a 17 base-pair DNA. Our results indicate that both the local folding and dynamic properties of Genesis are perturbed when it binds to the DNA site. Our data show that a conserved flexible amino acid sequence (wing 1) makes dynamic contacts to DNA in the complex and a short helix is induced by Genesis-DNA interactions. Our data indicate that, unlike the HNF-3gamma/DNA complex, a magnesium ion is not required in forming the stable Genesis-DNA complex.
[NMR paper] NMR assignments of the winged-helix domain of human werner syndrome protein.
NMR assignments of the winged-helix domain of human werner syndrome protein.
Related Articles NMR assignments of the winged-helix domain of human werner syndrome protein.
J Biomol NMR. 2005 Jul;32(3):261
Authors: Sun JZ, Feng HQ, Lin GX, Zeng W, Hu JS
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[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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Protein-ice interaction of an antifreeze protein observed with solid-state NMR [Chemi
Protein-ice interaction of an antifreeze protein observed with solid-state NMR
Siemer, A. B., Huang, K.-Y., McDermott, A. E....
Date: 2010-10-12
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions of proteins with their hydration shell and the ice lattice in frozen solution. We applied these methods to compare solvent interaction of an ice-binding...
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Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Related Articles Protein-ice interaction of an antifreeze protein observed with solid-state NMR.
Proc Natl Acad Sci U S A. 2010 Sep 30;
Authors: Siemer AB, Huang KY, McDermott AE
NMR on frozen solutions is an ideal method to study fundamental questions of macromolecular hydration, because the hydration shell of many biomolecules does not freeze together with bulk solvent. In the present study, we present previously undescribed NMR methods to study the interactions...
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[NMR paper] Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-s
Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-sweet analog. Evidence on the importance of residue AspB7 for sweet taste.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamic studies by NMR of the potent sweet protein monellin and a non-sweet analog. Evidence on the importance of residue AspB7 for sweet taste.
FEBS Lett. 1997 Aug 25;413(3):409-16
Authors: Mizukoshi T, Kohmura M, Suzuki E, Ariyoshi Y
Monellin, an...
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[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
Related Articles PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
Biochemistry. 1995 Sep 12;34(36):11617-24
Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B
Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
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[NMR paper] 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group rec
1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.
Related Articles 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.
Biochemistry. 1990 Oct 16;29(41):9623-31
Authors: Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG
The proton nuclear magnetic resonance spectra of the soluble fragment of native bovine and genetically engineered wild-type rat...
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[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA comple
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