[ASAP] Structural Basis for the Specific Cotranslational Incorporation of p-Boronophenylalanine into Biosynthetic Proteins
Structural Basis for the Specific Cotranslational Incorporation of p-Boronophenylalanine into Biosynthetic Proteins
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00171/20180424/images/medium/bi-2018-00171m_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00171
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04-25-2018 01:55 AM
Molecular Basis for the Attachment of S-Layer Proteins to the Cell Wall of Bacillus anthracis
Molecular Basis for the Attachment of S-Layer Proteins to the Cell Wall of Bacillus anthracis
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00060/20180314/images/medium/bi-2018-00060g_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00060
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nmrlearner
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03-15-2018 02:05 AM
[NMR paper] Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction.
Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction.
Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction.
Oncotarget. 2018 Jan 30;9(8):8068-8080
Authors: Verma A, Jing-Song F, Finch-Edmondson ML, Velazquez-Campoy A, Balasegaran S, Sudol M, Sivaraman J
Abstract
YES-associated protein (YAP) is a major effector protein of the Hippo tumor suppressor pathway, and is phosphorylated by the...
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03-01-2018 09:20 PM
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
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Structural basis for the interaction between the cell polarity proteins Par3 and Par6
Science
Cell types often exhibit asymmetric distributions of proteins, lipids, and organelles that are linked to specialized functions, and loss of polarization precedes pathological conditions such as cancer. The cell polarity proteins Par3 and Par6 and the ...
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02-14-2018 02:43 AM
[NMR paper] The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Here we introduce a thermodynamic framework, based on analysis of ITC and CD spectroscopy data, that provides experimental description of IDP association in terms of folding and binding contributions which can be predicted using sequence folding propensities and molecular modeling. We show how IDP can...
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09-15-2017 08:41 PM
[NMR paper] Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Related Articles Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Biochemistry. 2013 May 31;
Authors: Ali R, Kumar S, Balaram H, Sarma SP
Abstract
The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the...
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06-04-2013 06:31 PM
[NMR paper] Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Related Articles Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of Phospholipase D1 revealed by NMR spectroscopy.
Biochim Biophys Acta. 2013 Apr 19;
Authors: Farina B, Doti N, Pirone L, Malgieri G, Pedone EM, Ruvo M, Fattorusso R
Abstract
PED/PEA15 is a small protein involved in many protein-protein interactions that modulates the function of a number of key cellular effectors involved in...
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04-24-2013 09:48 PM
[NMR paper] Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue p
Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Related Articles Solvent polarity-dependent structural refolding: a CD and NMR study of a 15 residue peptide.
Proteins. 1995 Oct;23(2):196-203
Authors: Graf von Stosch A, Jiménez MA, Kinzel V, Reed J
A close association between the HIV surface protein gp120 and the CD4 T cell receptor initiates the viral multiplication cycle. A 15 amino acid peptide (LAV) within the CD4 binding domain of gp 120 has been shown to retain receptor binding ability. The...
Structural basis for the interaction between the cell polarity proteins Par3 and Par6 - Science
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