Membrane proteins are known to exert many essential biological functions by forming complexes in cell membranes. An example refers to the ?-barrel assembly machinery (BAM), a 200 kDa pentameric complex containing BAM proteins A-E that catalyzes the essential process of protein insertion into the outer membrane of gram-negative bacteria. While progress has been made in capturing three-dimensional structural snapshots of the BAM complex, the role of the lipoprotein BamC in the complex assembly in...
[NMR paper] A Free-Energy Landscape Analysis of Calmodulin Obtained from an NMR Data-Utilized Multi-Scale Divide-and-Conquer Molecular Dynamics Simulation
A Free-Energy Landscape Analysis of Calmodulin Obtained from an NMR Data-Utilized Multi-Scale Divide-and-Conquer Molecular Dynamics Simulation
Calmodulin (CaM) is a multifunctional calcium-binding protein, which regulates a variety of biochemical processes. CaM acts through its conformational changes and complex formation with its target enzymes. CaM consists of two globular domains (N-lobe and C-lobe) linked by an extended linker region. Upon calcium binding, the N-lobe and C-lobe undergo local conformational changes, followed by a major conformational change of the entire CaM to wrap the...
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11-27-2021 10:43 PM
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Characterization of Protein–Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements
Carl O?ster, Simone Kosol, Christoph Hartlmu?ller, Jonathan M. Lamley, Dinu Iuga, Andres Oss, Mai-Liis Org, Kalju Vanatalu, Ago Samoson, Tobias Madl and Jo?zef R. Lewandowski
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b03875/20170824/images/medium/ja-2017-038753_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b03875
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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08-25-2017 05:31 PM
[NMR paper] Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
Related Articles Characterization of protein-protein interfaces in large complexes by solid state NMR solvent paramagnetic relaxation enhancements.
J Am Chem Soc. 2017 Aug 07;:
Authors: Öster C, Kosol S, Hartlmüller C, Lamley JM, Iuga D, Oss A, Org ML, Vanatalu K, Samoson A, Madl T, Lewandowski JR
Abstract
Solid-state NMR is becoming a viable alternative for obtaining information about structures and...
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08-07-2017 07:31 PM
Variability and conservation of structural domains in divide-and-conquer approaches
Variability and conservation of structural domains in divide-and-conquer approaches
Abstract
The use of protein building blocks for the structure determination of multidomain proteins and proteinâ??protein complexes, also known as the â??divide and conquerâ?? approach, is an important strategy for obtaining protein structures. Atomic-resolution X-ray or NMR data of the individual domains are combined with lower-resolution electron microscopy maps or X-ray data of the full-length protein or the protein complex. Doing so, it is often assumed that the...
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05-30-2016 01:15 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I
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03-02-2011 02:01 AM
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 29;
Authors: Zhu J, Ye E, Terskikh V, Wu G
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08-17-2010 03:36 AM
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Solid-State (17)O NMR Spectroscopy of Large Protein-Ligand Complexes.
Angew Chem Int Ed Engl. 2010 Jul 28;
Authors: Zhu J, Ye E, Terskikh V, Wu G
Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes
Linear Mode
