NMR paper Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp

		BioNMR > Educational resources > Journal club
[NMR paper] Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

11-24-2010, 09:25 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,184

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

Conformational changes in a photosensory LOV domain monitored by time-resolved NMR sp

Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.

Related Articles Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy.

J Am Chem Soc. 2004 Mar 24;126(11):3390-1

Authors: Harper SM, Neil LC, Day IJ, Hore PJ, Gardner KH

Phototropins are light-activated kinases from plants that utilize light-oxygen-voltage (LOV) domains as blue light photosensors. Illumination of these domains leads to the formation of a covalent linkage between the protein and an internally bound flavin chromophore, destabilizing the surrounding protein and displacing an alpha-helix from its surface. Here we use a combination of spectroscopic tools to monitor the kinetic processes that spontaneously occur in the dark as the protein returns to the noncovalent ground state. Using time-resolved two-dimensional (2D) NMR methods, we measured the rate of this process at over 100 independent sites throughout the protein, establishing that regeneration of the dark state occurs cooperatively within a 1.6-fold range of observed rates. These data agree with other spectroscopic measurements of the kinetics of protein/FMN bond cleavage and global conformational changes, consistent with these processes experiencing a common rate-limiting step. Arrhenius analyses of the temperature dependence of these rates suggest that the transition state visited during this regeneration has higher energy than the denatured form of this protein domain despite the fact that there is no global unfolding of the domain during this process.

PMID: 15025443 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR Transient Enzyme–Substrate Recognition Monitored by Real-Time NMR Caroline Haupt, Rica Patzschke, Ulrich Weininger, Stefan Gro?ger, Michael Kovermann and Jochen Balbach http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2010048/aop/images/medium/ja-2011-010048_0002.gif Journal of the American Chemical Society DOI: 10.1021/ja2010048 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/nknzYbs0FNE	nmrlearner	Journal club	0	06-30-2011 05:01 AM
Transient enzyme-substrate recognition monitored by real-time NMR. Transient enzyme-substrate recognition monitored by real-time NMR. Transient enzyme-substrate recognition monitored by real-time NMR. J Am Chem Soc. 2011 Jun 10; Authors: Haupt C, Patzschke R, Weininger U, Gröger S, Kovermann M, Balbach J Slow protein folding processes during which kinetic folding intermediates occur for an extended time can lead to aggregation and dysfunction in living cells. Therefore protein folding helpers have evolved, which prevent proteins from aggregation and/ or speed up folding processes. In this study we present the...	nmrlearner	Journal club	0	06-15-2011 01:15 PM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy Abstract It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all detectable species. The analysis was carried out using experimental data obtained during aggregation of the 10.4 kDa Crh protein, which has been shown to involve a partially unfolded intermediate...	nmrlearner	Journal club	0	01-27-2011 04:31 AM
Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. Kinetic analysis of protein aggregation monitored by real-time 2D solid-state NMR spectroscopy. J Biomol NMR. 2011 Jan 21; Authors: Etzkorn M, Böckmann A, Baldus M It is shown that real-time 2D solid-state NMR can be used to obtain kinetic and structural information about the process of protein aggregation. In addition to the incorporation of kinetic information involving intermediate states, this approach can offer atom-specific resolution for all...	nmrlearner	Journal club	0	01-22-2011 01:52 PM
[NMR paper] Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange. Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange. Related Articles Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange. Biochemistry. 2005 May 31;44(21):7644-55 Authors: Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M The conformational stability of ribonuclease Sa (RNase Sa) has been measured at the per-residue level by NMR-monitored hydrogen exchange at pH* 5.5 and 30 degrees C. In these conditions, the exchange mechanism was found to be EXII. The conformational stability...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy. J Mol Biol. 2003 May 16;328(5):1161-71 Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation. Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation. Related Articles Micromixer-based time-resolved NMR: applications to ubiquitin protein conformation. Anal Chem. 2003 Feb 15;75(4):956-60 Authors: Kakuta M, Jayawickrama DA, Wolters AM, Manz A, Sweedler JV Time-resolved NMR spectroscopy is used to studychanges in protein conformation based on the elapsed time after a change in the solvent composition of a protein solution. The use of a micromixer and a continuous-flow method is described where the contents of...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[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

« 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