BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Unread 08-22-2010, 03:03 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,582
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin

Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.

Related Articles Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements.

Biochemistry. 1997 Apr 22;36(16):5029-44

Authors: Kelley JJ, Caputo TM, Eaton SF, Laue TM, Bushweller JH

NMR-based structure determination of Escherichia coli glutaredoxin-1 in its reduced and oxidized forms revealed only subtle structural differences between the two forms. In an effort to characterize the role dynamics may play in the functioning of the protein, the backbone dynamics of both the reduced and oxidized forms of E. coli glutaredoxin-1 have been characterized using inverse-detection two-dimensional 15N-1H NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation time constants and steady-state [1H]-15N NOEs were measured for a majority of the protonated backbone nitrogen atoms. These data were analyzed by using a model-free formalism to determine the generalized order parameter (S2), the effective correlation time for internal motions (tau(e)), 15N exchange broadening contributions (R(ex)), and the overall molecular rotational correlation time (tau(m)). Sedimentation equilibrium measurements showed the reduced protein to be monomeric whereas the oxidized form could be fit to a monomer-dimer equilibrium. In order to try and assess the effect of dimerization on the dynamical parameters, the measurements on the oxidized protein have been carried out at two concentrations with very different monomer/dimer ratios. There is increased motion on both nano-picosecond and micro-millisecond time scales in the reduced form relative to the oxidized form, consistent with a more rigid oxidized protein. The increase in motion in the reduced protein correlates with its decreased thermodynamic stability. The role of the observed differences in the dynamic behavior in the two forms, particularly in the active site, in glutaredoxin-1's role as a protein disulfide reductant is discussed.

PMID: 9125525 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR rela
Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR relaxation measurements. Related Articles Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR relaxation measurements. Biochemistry. 1999 Aug 3;38(31):9862-71 Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B The backbone dynamics of uniformly 15N-labeled reduced and oxidized putidaredoxin (Pdx) have been studied by 2D 15N NMR relaxation measurements. 15N T1 and T2 values and 1H-15N NOEs have been measured for the diamagnetic...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 vi
Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications. Related Articles Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications. Biochemistry. 1998 Sep 1;37(35):12320-30 Authors: Banci L, Bertini I, Cavazza C, Felli IC, Koulougliotis D Rotating frame 15N relaxation NMR experiments have been performed to study the local mobility of the...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin
Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements. Biochemistry. 1997 Apr 22;36(16):5029-44 Authors: Kelley JJ, Caputo TM, Eaton SF, Laue TM, Bushweller JH NMR-based structure determination of Escherichia coli glutaredoxin-1 in its reduced...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments
Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Glutaredoxin-3 from Escherichia coli. Amino acid sequence, 1H AND 15N NMR assignments, and structural analysis. J Biol Chem. 1996 Mar 22;271(12):6736-45 Authors: Aslund F, Nordstrand K, Berndt KD, Nikkola M, Bergman T, Ponstingl H, Jörnvall H, Otting G, Holmgren A The primary and...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Esc
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. Related Articles Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. Biochemistry. 1993 Jan 19;32(2):426-35 Authors: Stone MJ, Chandrasekhar K, Holmgren A, Wright PE, Dyson HJ The backbone and tryptophan side-chain dynamics of both the reduced and oxidized forms of uniformly 15N-labeled Escherichia...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. c
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. 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 NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci. 1992...
nmrlearner Journal club 0 08-21-2010 11:41 PM
[NMR paper] Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxi
Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin. FEBS Lett. 1991 Jun 24;284(2):178-83 Authors: Chandrasekhar K, Krause G, Holmgren A, Dyson HJ As a necessary first step in the use of heteronuclear correlated spectra to obtain high resolution solution structures of the protein, assignment of the...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex:
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism. J Mol Biol. 1999 Feb 19;286(2):541-52 Authors: Nordstrand K, slund F, Holmgren A, Otting G, Berndt KD Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of...
nmrlearner Journal club 0 08-21-2010 04:03 PM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2017, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 05:28 AM.


Map