[NMR paper] Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Biochim Biophys Acta. 2014 Nov 22;
Authors: Kim JH, Bothe JR, Reid Alderson T, Markley JL
Abstract
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have...
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12-03-2014 04:05 PM
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Publication date: Available online 22 November 2014
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Jin Hae Kim , Jameson R. Bothe , T. Reid Alderson , John L. Markley</br>
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have evolved machinery consisting of specialized proteins that operate together to assemble...
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11-22-2014 01:48 PM
[NMR paper] Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein.
Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein.
Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein.
PLoS One. 2014;9(6):e100564
Authors: Tossavainen H, Kukkurainen S, Määttä JA, Kähkönen N, Pihlajamaa T, Hytönen VP, Kulomaa MS, Permi P
Abstract
Chimeric avidin (ChiAVD) is a product of rational protein engineering remarkably resistant to heat and harsh conditions. In quest of the fundamentals behind factors affecting stability we have...
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Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
Related Articles NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....
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[NMR paper] Dissecting functional interactions in coagulation protein complexes by use of NMR spe
Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Related Articles Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.
Curr Protein Pept Sci. 2002 Jun;3(3):275-85
Authors: Tolkatchev D, Koutychenko A, Ni F
The blood coagulation cascade can be considered as a system of well-orchestrated protein activation reactions involving and leading to the formation of large macromolecular assemblies. NMR investigations performed during the last six years have focused...
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11-24-2010 08:49 PM
[NMR paper] NMR for the design of functional mimetics of protein-protein interactions: one key is
NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges.
Related Articles NMR for the design of functional mimetics of protein-protein interactions: one key is in the building of bridges.
Biochem Cell Biol. 1998;76(2-3):177-88
Authors: Song J, Ni F
Using the design of bivalent and bridge-binding inhibitors of thrombin as an example, we review an NMR-based experimental approach for the design of functional mimetics of protein-protein interactions. The strategy includes: (i) identification...
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11-17-2010 11:06 PM
[NMR paper] Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxy
Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
Biochemistry. 1997 Dec 2;36(48):14676-82
Authors: Reddy DV, Shenoy BC, Carey PR, Sönnichsen FD
Transcarboxylase (TC) is a biotin-containing enzyme catalyzing the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form...
Self-Assembly of a Functional Triple Protein: Hemoglobin-Avidin-Hemoglobinvia Biotin–Avidin Interactions
Linear Mode
