NMR paper NMR and protein folding: equilibrium and stopped-flow studies.

		BioNMR > Educational resources > Journal club
[NMR paper] NMR and protein folding: equilibrium and stopped-flow studies.

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

08-22-2010, 03:01 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

NMR and protein folding: equilibrium and stopped-flow studies.

NMR and protein folding: equilibrium and stopped-flow studies.

Related Articles NMR and protein folding: equilibrium and stopped-flow studies.

Protein Sci. 1993 Dec;2(12):2007-14

Authors: Frieden C, Hoeltzli SD, Ropson IJ

NMR studies are now unraveling the structure of intermediates of protein folding using hydrogen-deuterium exchange methodologies. These studies provide information about the time dependence of formation of secondary structure. They require the ability to assign specific resonances in the NMR spectra to specific amide protons of a protein followed by experiments involving competition between folding and exchange reactions. Another approach is to use 19F-substituted amino acids to follow changes in side-chain environment upon folding. Current techniques of molecular biology allow assignments of 19F resonances to specific amino acids by site-directed mutagenesis. It is possible to follow changes and to analyze results from 19F spectra in real time using a stopped-flow device incorporated into the NMR spectrometer.

PMID: 8298453 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14 Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...	nmrlearner	Journal club	0	11-24-2010 08:49 PM
[NMR paper] Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions. Related Articles Stopped-flow NMR measurement of hydrogen exchange rates in reduced horse cytochrome c under strongly destabilizing conditions. Proteins. 1998 Aug 1;32(2):241-7 Authors: Bhuyan AK, Udgaonkar JB A procedure to measure exchange rates of fast exchanging protein amide hydrogens by time-resolved NMR spectroscopy following in situ initiation of the reaction by diluting a native protein solution into an...	nmrlearner	Journal club	0	11-17-2010 11:15 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 tweet] Dynamic studies of phloem and xylem flow in fully differentiated plants by fast nucle Dynamic studies of phloem and xylem flow in fully differentiated plants by fast nuclear-magnetic-resonance microima... http://ping.fm/nfA2k Published by stevenbird64 (Steven Bird) on 2010-10-03T16:25:36Z Source: Twitter	nmrlearner	Twitter NMR	0	10-03-2010 04:58 PM
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machiner Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machineries * In the context of a project funded by European Research Council, two postdoctoral positions are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS. * The laboratory host… More...	nmrlearner	Job marketplace	0	09-11-2010 01:25 AM
[NMR paper] NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins. NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins. Related Articles NMR and stopped-flow studies of metal ion binding to alpha-lactalbumins. Biochim Biophys Acta. 1996 Mar 7;1293(1):72-82 Authors: Aramini JM, Hiraoki T, Grace MR, Swaddle TW, Chiancone E, Vogel HJ 1H-NMR spectroscopy and stopped-flow techniques have been used to investigate the binding of a host of metal ions to alpha-lactalbumins from bovine, goat, and human sources. We have identified two 1H-NMR markers diagnostic of metal ion binding to the...	nmrlearner	Journal club	0	08-22-2010 02:27 PM
[NMR paper] Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labele Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Stopped-flow NMR spectroscopy: real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9318-22 Authors: Hoeltzli SD, Frieden C Escherichia coli dihydrofolate reductase (DHFR; EC 1.5.1.3) contains...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] Prelude to NMR studies of protein folding. Prelude to NMR studies of protein folding. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Prelude to NMR studies of protein folding. Nat Struct Biol. 1999 Jul;6(7):608 Authors: Smith T	nmrlearner	Journal club	0	08-21-2010 04:03 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