The endoplasmic reticulum transmembrane protein vesicle-associated membrane protein-associated protein (VAP) plays a central role in the formation and function of membrane contact sites (MCS) through its interactions with proteins. The major sperm protein (MSP) domain of VAP binds to a variety of sequences which are referred to as FFAT-like motifs. In this study, we investigated the interactions of eight peptides containing FFAT-like motifs with the VAP-A MSP domain (VAP-A(MSP) ) by solution...
[ASAP] Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
Extratelomeric Binding of the Telomere Binding Protein TRF2 at the PCGF3 Promoter Is G-Quadruplex Motif-Dependent
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00019/20180410/images/medium/bi-2018-00019w_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00019
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nmrlearner
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04-12-2018 01:01 AM
Influence of Quasi-Specific Sites on Kinetics of TargetDNA Search by a Sequence-Specific DNA-Binding Protein
Influence of Quasi-Specific Sites on Kinetics of TargetDNA Search by a Sequence-Specific DNA-Binding Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00967/20151103/images/medium/bi-2015-009678_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00967
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11-09-2015 05:03 PM
Speeding up sequence specific assignment of IDPs
Speeding up sequence specific assignment of IDPs
Abstract The characterization of intrinsically disordered proteins (IDPs) by NMR spectroscopy is made difficult by the extensive spectral overlaps. To overcome the intrinsic low-resolution of the spectra the introduction of high-dimensionality experiments is essential. We present here a set of high-resolution experiments based on direct 13C-detection which proved useful in the assignment of α-synuclein, a paradigmatic IDP. In particular, we describe the implementation of 4D HCBCACON, HCCCON, HCBCANCO, 4/5D HNCACON and HNCANCO and 3/4D...
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06-13-2012 11:59 PM
[NMR paper] NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zin
NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Related Articles NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Proteins. 2002 Nov 1;49(2):289-93
Authors: Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA
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11-24-2010 08:58 PM
[NMR paper] NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
Related Articles NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
J Inorg Biochem. 2000 Apr;79(1-4):365-70
Authors: Hannan JP, Whittaker SB, Hemmings AM, James R, Kleanthous C, Moore GR
The 134 amino acid DNase domain of colicin E9 contains a zinc-finger-like HNH motif that binds divalent transition metal ions. We have used 1D 1H and 2D 1H-15N NMR methods to characterise the binding of Co2+, Ni2+ and Zn2+ to this protein. Data for the...
nmrlearner
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11-18-2010 09:15 PM
[NMR paper] Sequence-specific NMR assignments of the trp repressor from Escherichia coli using th
Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
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 Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
Eur J Biochem. 1992 Feb 15;204(1):137-46
Authors: Borden KL, Bauer CJ, Frenkiel TA, Beckmann P, Lane AN
...
nmrlearner
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08-21-2010 11:41 PM
[NMR paper] A relational database for sequence-specific protein NMR data.
A relational database for sequence-specific protein NMR data.
Related Articles A relational database for sequence-specific protein NMR data.
J Biomol NMR. 1991 Sep;1(3):217-36
Authors: Seavey BR, Farr EA, Westler WM, Markley JL
A protein NMR database has been designed and is being implemented. The database is intended to contain solution NMR results from proteins and peptides (larger than 12 residues). A relational database format has been chosen that indexes data by: primary journal citation, molecular species, sequence-related and...
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08-21-2010 11:12 PM
[NMR paper] Sequence-specific 1H NMR assignments and determination of the secondary structure for
Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Related Articles Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Biochemistry. 1990 Aug 14;29(32):7515-22
Authors: Vendrell J, Wider G, Avilés FX, Wüthrich K
Nearly complete sequence-specific 1H NMR assignments are presented for amino acid residues 3-81 in the 81-residue globular...