Publication date: Available online 27 July 2013 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Christopher A. Waudby , Hélène Launay , Lisa D. Cabrita , John Christodoulou
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution. In recent years NMR methods have also been developed to study protein folding as it might occur within the cell, in a de novo manner, by observing the folding of nascent polypeptides in the process of emerging from the ribosome during synthesis. Despite the 2.3 MDa molecular weight of the bacterial 70S ribosome, many nascent polypeptides, and some ribosomal proteins, have sufficient local flexibility that sharp resonances may be observed in solution-state NMR spectra. In providing information on dynamic regions of the structure, NMR spectroscopy is therefore highly complementary to alternative methods such as X-ray crystallography and cryo-electron microscopy, which have successfully characterized the rigid core of the ribosome particle. However, the low working concentrations and limited sample stability associated with ribosome-nascent chain complexes means that such studies still present significant technical challenges to the NMR spectroscopist. This review will discuss the progress that has been made in this area, surveying all NMR studies that have been published to date, and with a particular focus on strategies for improving experimental sensitivity. Graphical abstract
[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...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] Unfolded proteins and protein folding studied by NMR.
Unfolded proteins and protein folding studied by NMR.
Related Articles Unfolded proteins and protein folding studied by NMR.
Chem Rev. 2004 Aug;104(8):3607-22
Authors: Dyson HJ, Wright PE
nmrlearner
Journal club
0
11-24-2010 10:01 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...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly
NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
Related Articles NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
J Mol Biol. 2002 Oct 11;323(1):143-51
Authors: Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F
L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Kinetic studies of protein folding using NMR spectroscopy.
Kinetic studies of protein folding using NMR spectroscopy.
Related Articles Kinetic studies of protein folding using NMR spectroscopy.
Nat Struct Biol. 1998 Jul;5 Suppl:504-7
Authors: Dobson CM, Hore PJ
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR.
Annu Rev Biophys Biomol Struct. 1992;21:243-65
Authors: Englander SW, Mayne L
HX-labeling experiments in the pH-pulse mode show that protein folding can be remarkably fast. A near-native form can be reached within milliseconds. Experimental analysis of...
Protein folding on the ribosome studied using NMR spectroscopy
Highlights
Linear Mode
