NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Adina M. Kilpatrick, C. Andrew Fowler, Theodore Gurrola, Jerry E. Honts</br>
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02-17-2016 07:50 PM
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Aromatic spectral editing Techniques for magic-Angle-spinning solid-state NMR spectroscopy of uniformly 13C-labeled proteins
Publication date: Available online 14 September 2015
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Jonathan K. Williams, Klaus Schmidt-Rohr, Mei Hong</br>
The four aromatic amino acids in proteins, namely histidine, phenylalanine, tyrosine, and tryptophan, give highly overlapped 13C chemical shifts between 100 and 160ppm, and have so far been largely neglected in solid-state NMR determination of protein structures. Yet...
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09-14-2015 10:42 PM
Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Adedolapo Ojoawo , Choua Xiong , Kim N. Ha</br>
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01-29-2014 12:50 AM
[NMR paper] NMR studies of a new family of DNA binding proteins: the THAP proteins.
NMR studies of a new family of DNA binding proteins: the THAP proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR studies of a new family of DNA binding proteins: the THAP proteins.
J Biomol NMR. 2013 Jan 11;
Authors: Gervais V, Campagne S, Durand J, Muller I, Milon A
Abstract
The THAP (THanatos-Associated Protein) domain is an evolutionary conserved C2CH zinc-coordinating domain shared with a large family of cellular factors (THAP proteins)....
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02-03-2013 10:22 AM
[NMR paper] Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
PLoS One. 2013;8(1):e53639
Authors: Dai K, Liao S, Zhang J, Zhang X, Tu X
Abstract
The ADF/cofilin family has been characterized as a group of actin-binding...
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02-03-2013 10:19 AM
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
Biochemistry. 2011 Jan 12;
Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
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01-14-2011 12:05 PM
[NMR paper] NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: c
NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Related Articles NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Biochemistry. 2005 Mar 15;44(10):3708-17
Authors: Volpon L, D'Orso I, Young CR, Frasch AC, Gehring K
TcUBP1 is a trypanosome cytoplasmic RNA-binding protein containing a single, conserved RNA-recognition motif (RRM) domain involved in selective destabilization of U-rich...
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11-24-2010 11:14 PM
[NMR paper] NMR structural studies on antifreeze proteins.
NMR structural studies on antifreeze proteins.
Related Articles NMR structural studies on antifreeze proteins.
Biochem Cell Biol. 1998;76(2-3):284-93
Authors: Sönnichsen FD, Davies PL, Sykes BD
Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of approximately 1 degree C, which is sufficient to...