Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing and filtering strategies underlie these powerful methodologies. Approaches to the characterization of the dynamics of protein complexes have also matured to the point where detailed studies of the effects of complexation on dynamics can be studied over a wide range of timescales.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
Prog Nucl Magn Reson Spectrosc. 2011 Feb;58(1-2):1-61
Authors: Dominguez C, Schubert M, Duss O, Ravindranathan S, Allain FH
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01-19-2011 11:18 AM
[NMR paper] Millisecond protein folding studied by NMR spectroscopy.
Millisecond protein folding studied by NMR spectroscopy.
Related Articles Millisecond protein folding studied by NMR spectroscopy.
Protein Pept Lett. 2005 Feb;12(2):139-46
Authors: Zeeb M, Balbach J
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond...
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11-24-2010 11:14 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
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11-24-2010 10:01 PM
[NMR paper] Complexes of photosynthetic redox proteins studied by NMR.
Complexes of photosynthetic redox proteins studied by NMR.
Related Articles Complexes of photosynthetic redox proteins studied by NMR.
Photosynth Res. 2004;81(3):277-87
Authors: Ubbink M
In the photosynthetic redox chain, small electron transfer proteins shuttle electrons between the large membrane-associated redox complexes. Short-lived but specific protein:protein complexes are formed to enable fast electron transfer. Recent nuclear magnetic resonance (NMR) studies have elucidated the binding sites on plastocyanin, cytochrome c (6) and...
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Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 6 October 2010</br>
Cyril, Dominguez , Mario, Schubert , Olivier, Duss , Sapna, Ravindranathan , Frédéric H.-T., Allain</br>
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10-07-2010 02:32 PM
[NMR paper] Conformational differences between complexes of elongation factor Tu studied 19F-NMR
Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
Eur J Biochem. 1993 Dec 15;218(3):1041-7
Authors: Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J
An analogue of elongation factor Tu (EF-Tu) from Escherichia coli was prepared by...
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08-22-2010 03:01 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
Protein complexes studied by NMR spectroscopy.
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