Large oligomeric enzymes control a myriad of cellular processes, from protein synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase, a prototypical protease important for cellular homeostasis, degrades peptides within a ca. 60 Ĺ wide tetrahedral chamber with four lateral openings. The mechanisms of substrate trafficking and processing remain debated. Here, we integrate magic-angle spinning (MAS) NMR, mutagenesis, co-evolution analysis and molecular dynamics simulations...
[NMR paper] Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.
Biophys J. 2016 Jan 19;110(2):372-381
Authors: Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R
Abstract
Here, we present a structural and dynamic description of CBP-ID4 at atomic resolution. ID4 is the fourth intrinsically disordered linker of CREB-binding protein (CBP). In spite of the...
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Closing the Loop on an HIV Escape Mechanism - Infection Control Today
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Closing the Loop on an HIV Escape Mechanism
Infection Control Today
They used a combination of high-tech tools and techniques, including magic-angle-spinning nuclear magnetic resonance (NMR) spectroscopy and computer simulations of molecules, to examine the interactions between HIV and the host-cell protein ...
Closing the Loop on an HIV Escape Mechanism - Infection Control Today
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[NMR paper] Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.
Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.
Related Articles Functional Dynamics of Deuterated ?2 -Adrenergic Receptor in Lipid Bilayers Revealed by NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Oct 3;
Authors: Kofuku Y, Ueda T, Okude J, Shiraishi Y, Kondo K, Mizumura T, Suzuki S, Shimada I
Abstract
G-protein-coupled receptors (GPCRs) exist in conformational equilibrium between active and inactive states, and the former population determines the efficacy of...
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10-07-2014 02:31 PM
[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Related Articles Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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Functional dynamics of proteins revealed by solution NMR
Functional dynamics of proteins revealed by solution NMR
October 2012
Publication year: 2012
Source:Current Opinion in Structural Biology, Volume 22, Issue 5</br>
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Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation...
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Self-Assembly of Flexible?-Strands into ImmobileAmyloid-Like ?-Sheets in MembranesAs Revealed by Solid-State 19F NMR
Self-Assembly of Flexible?-Strands into ImmobileAmyloid-Like ?-Sheets in MembranesAs Revealed by Solid-State 19F NMR
Parvesh Wadhwani, Erik Strandberg, Nico Heidenreich, Jochen Bu?rck, Susanne Fangha?nel and Anne S. Ulrich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja301328f/aop/images/medium/ja-2012-01328f_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja301328f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/dpJwN953qQE
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[NMR paper] NMR structures of loop B RNAs from the stem-loop IV domain of the enterovirus interna
NMR structures of loop B RNAs from the stem-loop IV domain of the enterovirus internal ribosome entry site: a single C to U substitution drastically changes the shape and flexibility of RNA.
Related Articles NMR structures of loop B RNAs from the stem-loop IV domain of the enterovirus internal ribosome entry site: a single C to U substitution drastically changes the shape and flexibility of RNA.
Biochemistry. 2004 May 18;43(19):5757-71
Authors: Du Z, Ulyanov NB, Yu J, Andino R, James TL
The 5'-untranslated region of positive-strand RNA viruses...
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[NMR paper] Structure of an RNA hairpin loop with a 5'-CGUUUCG-3' loop motif by heteronuclear NMR
Structure of an RNA hairpin loop with a 5'-CGUUUCG-3' loop motif by heteronuclear NMR spectroscopy and distance geometry.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure of an RNA hairpin loop with a 5'-CGUUUCG-3' loop motif by heteronuclear NMR spectroscopy and distance geometry.
Biochemistry. 1997 Nov 18;36(46):13989-4002
Authors: Sich C, Ohlenschläger O, Ramachandran R, Görlach M, Brown LR
Structural features of a 19-nucleotide RNA hairpin loop (5'-GGCGUACGUUUCGUACGCC-3'),...
Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
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