Related ArticlesDemonstration by NMR of folding domains in lysozyme.
Nature. 1991 Feb 14;349(6310):633-6
Authors: Miranker A, Radford SE, Karplus M, Dobson CM
Although there has been much speculation on the pathways of protein folding, only recently have experimental data on the topic been available. The study of proteins under conditions where species intermediate between the fully folded and unfolded states are stable has provided important information, for example about the disulphide intermediates in BPTI, cis/trans proline isomers of RNase A3 and the molten globule state of alpha-lactalbumin. An alternative approach to investigating folding pathways has involved detection and characterization of transient conformers in refolding studies using stopped-flow methods coupled with NMR measurements of hydrogen exchange. The formation of intermediate structures has been detected in the early stages of folding of cytochrome c, RNaseA and barnase. For alpha-lactalbumin, hydrogen exchange kinetics monitored by NMR proved to be crucial for identifying native-like structural features in the stable molten globule state. An analogous partially folded protein stable under equilibrium conditions has not been observed for the structurally homologous protein hen egg-white lysozyme, although there is evidence that a similar but transient state is formed during refolding. Here we describe NMR experiments based on competition between hydrogen exchange and the refolding process which not only support the existence of such a transient species for lysozyme, but enable its structural characteristics to be defined. The results indicate that the two structural domains of lysozyme are distinct folding domains, in that they differ significantly in the extent to which compact, probably native-like, structure is present in the early stages of folding.
[NMR900 blog] picoSpin Benchtop NMR Spectrometer - Demonstration
picoSpin Benchtop NMR Spectrometer - Demonstration
Cole-Parmer Canada will be hosting a live demonstration of the picoSpin, the world's first commercial miniature FT-NMR spectrometer. Two demonstrations are scheduled, one in Montreal on October 4th, 2011 and one in Toronto on October 5th. There is no cost to attend the event, and complimentary snacks and beverages will be served. Please contact Roberto Santana at 514-355-6100 ext. 250 or (rsantana "at" coleparmer.ca) for more information and to reserve your spot.
If there will be enough interest, an additional demonstration is possible...
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09-09-2011 08:41 AM
[NMR paper] Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Related Articles Diffusion NMR spectroscopy: folding and aggregation of domains in p53.
Chembiochem. 2005 Sep;6(9):1550-65
Authors: Dehner A, Kessler H
Protein interactions and aggregation phenomena are probably amongst the most ubiquitous types of interactions in biological systems; they play a key role in many cellular processes. The ability to identify weak intermolecular interactions is a unique feature of NMR spectroscopy. In recent years, pulsed-field gradient NMR...
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12-01-2010 06:56 PM
[NMR paper] NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Related Articles NMR investigation of main-chain dynamics of the H80E mutant of bovine neurophysin-I: demonstration of dimerization-induced changes at the hormone-binding site.
Biochemistry. 2005 Sep 6;44(35):11766-76
Authors: Naik MT, Lee H, Bracken C, Breslow E
Neurophysins are hormone-binding proteins composed of two partially homologous domains. Ligand-binding (localized to the...
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12-01-2010 06:56 PM
[NMR paper] Remodeling of HDL by phospholipid transfer protein: demonstration of particle fusion
Remodeling of HDL by phospholipid transfer protein: demonstration of particle fusion by 1H NMR spectroscopy.
Related Articles Remodeling of HDL by phospholipid transfer protein: demonstration of particle fusion by 1H NMR spectroscopy.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):910-6
Authors: Korhonen A, Jauhiainen M, Ehnholm C, Kovanen PT, Ala-Korpela M
There is evidence that phospholipid transfer protein (PLTP) can increase reverse cholesterol transport by inducing favorable subclass distribution in the high density lipoprotein (HDL)...
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11-17-2010 11:15 PM
[NMR paper] Demonstration of protein-protein interaction specificity by NMR chemical shift mappin
Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.
Protein Sci. 1997 Dec;6(12):2624-7
Authors: Rajagopal P, Waygood EB, Reizer J, Saier MH, Klevit RE
...
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08-22-2010 05:08 PM
[NMR paper] Demonstration of positionally disordered water within a protein hydrophobic cavity by
Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Related Articles Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Science. 1995 Mar 24;267(5205):1813-7
Authors: Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM
The presence and location of water of hydration (that is, bound water) in the solution structure of human interleukin-1 beta (hIL-1 beta) was investigated with water-selective two-dimensional heteronuclear magnetic resonance spectroscopy. It is shown...
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08-22-2010 03:41 AM
[NMR paper] Detection and characterization of an early folding intermediate of T4 lysozyme using
Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Related Articles Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little...
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08-21-2010 11:41 PM
[NMR paper] 31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Esc
31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl.
Related Articles 31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl.
J Biol Chem. 1991 Apr 15;266(11):6690-2
Authors: Pas HH, Meyer GH, Kruizinga WH, Tamminga KS, van Weeghel RP, Robillard GT
The mannitol-specific phosphotransferase system transport protein, Enzyme IIMtl, contains two catalytically important phosphorylated amino acid...
Demonstration by NMR of folding domains in lysozyme.
Linear Mode
