NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
NMR assignment and secondary structure of the C-terminal DNA binding domain of Arabidopsis thaliana VERNALIZATION1.
Biomol NMR Assign. 2011 May 8;
Authors: Mylne JS, Mas C, Hill JM
VERNALIZATION1 (VRN1) is a multidomain DNA binding protein from Arabidopsis thaliana that is required for the acceleration of flowering time in response to prolonged cold treatment; a physiological process called vernalization. VRN1 is a 39*kDa protein...
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[NMR paper] NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
Related Articles NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
J Biomol NMR. 2005 Aug;32(4):339
Authors: Taylor JD, Fawaz RR, Ababou A, Williams MA, Ladbury JE
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[NMR paper] NMR backbone assignment of a protein kinase catalytic domain by a combination of seve
NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase.
Related Articles NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase.
Chembiochem. 2004 Nov 5;5(11):1508-16
Authors: Langer T, Vogtherr M, Elshorst B, Betz M, Schieborr U, Saxena K, Schwalbe H
Protein phosphorylation is one of the most important mechanisms...
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[NMR paper] NMR assignment and structural characterization of the fatty acid binding protein from
NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
Related Articles NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
J Biomol NMR. 2003 Apr;25(4):355-6
Authors: Lücke C, Kizilbash N, van Moerkerk HT, Veerkamp JH, Hamilton JA
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[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in
NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
Related Articles NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation.
J Biomol NMR. 2002 Jun;23(2):151-2
Authors: Espejo F, Green M, Preece NE, Assa-Munt N
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[NMR paper] NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
Related Articles NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
J Biomol NMR. 2001 Jan;19(1):79-80
Authors: Horst R, Damberger F, Peng G, Nikonova L, Leal WS, Wüthrich K
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
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[NMR paper] 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secon
1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
Related Articles 1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
J Biomol NMR. 1993 Nov;3(6):613-26
Authors: Eriksson PO, Sahlman L
The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the...
NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
Linear Mode
