NMR paper Demonstration by NMR of folding domains in lysozyme.

		BioNMR > Educational resources > Journal club
[NMR paper] Demonstration by NMR of folding domains in lysozyme.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-21-2010, 11:16 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,776

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Demonstration by NMR of folding domains in lysozyme.

Demonstration by NMR of folding domains in lysozyme.

Related Articles Demonstration 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.

PMID: 2000138 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[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...	nmrlearner	News from NMR blogs	0	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...	nmrlearner	Journal club	0	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...	nmrlearner	Journal club	0	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)...	nmrlearner	Journal club	0	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 ...	nmrlearner	Journal club	0	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...	nmrlearner	Journal club	0	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...	nmrlearner	Journal club	0	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...	nmrlearner	Journal club	0	08-21-2010 11:16 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off