[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition.
Sequential protein NMR assignments in the liquid state via sequential data acquisition.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Sequential protein NMR assignments in the liquid state via sequential data acquisition.
J Magn Reson. 2013 Dec 14;239C:23-28
Authors: Wiedemann C, Bellstedt P, Kirschstein A, Häfner S, Herbst C, Görlach M, Ramachandran R
Abstract
Two different NMR pulse schemes involving sequential (1)H data acquisition are...
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[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition
Sequential protein NMR assignments in the liquid state via sequential data acquisition
Publication date: Available online 14 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Christoph Wiedemann , Peter Bellstedt , Anika Kirschstein , Sabine Häfner , Christian Herbst , Matthias Görlach , Ramadurai Ramachandran</br>
Two different NMR pulse schemes involving sequential 1H data acquisition are presented for achieving protein backbone sequential resonance assignments: (i) acquisition of 3D {HCCNH & HNCACONH} and (ii) collection of 3D {HNCOCANH &...
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[NMR paper] NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Related Articles NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Biochemistry. 2005 Sep 6;44(35):11766-76
Authors: Naik MT, Lee H, Bracken C, Breslow E
Neurophysins are hormone-binding proteins composed of two partially homologous domains. Ligand-binding (localized to the...
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12-01-2010 06:56 PM
[NMR paper] Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp
Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
Related Articles Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.
J Am Chem Soc. 2004 Mar 24;126(11):3390-1
Authors: Harper SM, Neil LC, Day IJ, Hore PJ, Gardner KH
Phototropins are light-activated kinases from plants that utilize light-oxygen-voltage (LOV) domains as blue light photosensors. Illumination of these domains leads to the formation of a covalent linkage between the protein and an...
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11-24-2010 09:25 PM
[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
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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...
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08-22-2010 03:01 AM
[NMR paper] NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N as
NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Related Articles NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Biochemistry. 1993 Jun 15;32(23):6032-40
Authors: Cox M, Dekker N, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R
The 1H and 15N resonances of the POU-specific DNA-binding domain of transcription factor Oct-1 have been assigned sequentially using two-dimensional homo- and heteronuclear...
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08-21-2010 11:53 PM
[NMR paper] Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from p
Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Related Articles Sequential 1H NMR assignments and secondary structure of an IgG-binding domain from protein G.
Biochemistry. 1991 Jun 4;30(22):5335-40
Authors: Lian LY, Yang JC, Derrick JP, Sutcliffe MJ, Roberts GC, Murphy JP, Goward CR, Atkinson T
Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6988, which retains IgG-binding activity, has been...
Sequential DNA Binding and Dimerization Processesof the Photosensory Protein EL222
Linear Mode
