[NMR paper] NMR assignment of the gpU tail protein from lambda bacteriophage.
NMR assignment of the gpU tail protein from lambda bacteriophage.
Related Articles NMR assignment of the gpU tail protein from lambda bacteriophage.
J Biomol NMR. 2005 May;32(1):91-2
Authors: Edmonds L, Thirumoorthy R, Liu A, Davidson A, Donaldson L
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11-25-2010 08:21 PM
[NMR paper] NMR solution structure and topological orientation of monomeric phospholamban in dode
NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Related Articles NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles.
Biophys J. 2003 Oct;85(4):2589-98
Authors: Zamoon J, Mascioni A, Thomas DD, Veglia G
Phospholamban is an integral membrane protein that regulates the contractility of cardiac muscle by maintaining cardiomyocyte calcium homeostasis. Abnormalities in association of protein kinase A with PLB have recently...
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[NMR paper] Characterization of the monomeric form of the transmembrane and cytoplasmic domains o
Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Related Articles Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin beta 3 subunit by NMR spectroscopy.
Biochemistry. 2002 Dec 31;41(52):15618-24
Authors: Li R, Babu CR, Valentine K, Lear JD, Wand AJ, Bennett JS, DeGrado WF
We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and...
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[NMR paper] Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
Related Articles Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
J Biol Chem. 2002 Apr 5;277(14):12375-81
Authors: Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G
Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent...
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[NMR paper] NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein i
NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Related Articles NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Biochemistry. 1998 Jun 30;37(26):9316-22
Authors: Qian H, Sahlman L, Eriksson PO, Hambraeus C, Edlund U, Sethson I
Mercuric ions are toxic to living organisms because of their strong affinity for cysteine residues in proteins. Some bacteria have developed a resistance...
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[NMR paper] NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of
NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
Related Articles NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
Cell. 1998 Apr 17;93(2):289-99
Authors: Legault P, Li J, Mogridge J, Kay LE, Greenblatt J
The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage lambda and boxB RNA was determined by heteronuclear magnetic resonance...
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[NMR paper] Structure and stability of monomeric lambda repressor: NMR evidence for two-state fol
Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Related Articles Structure and stability of monomeric lambda repressor: NMR evidence for two-state folding.
Biochemistry. 1995 Mar 28;34(12):3884-92
Authors: Huang GS, Oas TG
The absence of equilibrium intermediates in protein folding reactions (i.e., two-state folding) simplifies thermodynamic and kinetic analyses but is difficult to prove rigorously. We demonstrate a sensitive method for detecting partially folded species based on using proton chemical...
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[NMR paper] Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbon
Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.
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 Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.
Eur J Biochem. 1999 Mar;260(2):347-54
Authors: ...