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 11-24-2010, 08:58 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,137
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 Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and el

Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and electronic absorbance study.

Related Articles Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A (1)H-NMR and electronic absorbance study.

Protein Sci. 2002 Sep;11(9):2273-8

Authors: Castelli DD, Lovera E, Ascenzi P, Fasano M

The effect of urea concentration on the backbone solution structure of the cyanide derivative of ferric Caretta caretta myoglobin (at pH 5.4) is reported. By addition of urea, sequential and long-range nuclear Overhauser effects (NOEs) are gradually lost. By using the residual NOE constraints to build the molecular model, a picture of the unfolding pathway was obtained. When the urea concentration is raised to 2.2 M, helices A and B appear largely disordered; helices C, D, and F loose structural constraints at 3.0 M urea. At urea concentration >6 M, the protein appears to be fully unfolded, including the GH hairpin and helix E stabilizing the prosthetic group. Reversible and cooperative denaturation isotherms obtained by following NOE peaks are considerably different from those obtained by monitoring electronic absorption changes. The reversible and cooperative urea-dependent folding-unfolding process of C. caretta myoglobin follows the minimum three-state mechanism N long left and right arrow X long left and right arrow D, where X represents a disordered globin structure (occurring at approximately 4 M urea) that still binds the heme.

PMID: 12192083 [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] NMR assignment of the turtle prion protein fragment tPrP(121-225).
NMR assignment of the turtle prion protein fragment tPrP(121-225). Related Articles NMR assignment of the turtle prion protein fragment tPrP(121-225). J Biomol NMR. 2004 Sep;30(1):97 Authors: Calzolai L, Lysek DA, Wüthrich K
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] 1H NMR structure of the heme pocket of HNO-myoglobin.
1H NMR structure of the heme pocket of HNO-myoglobin. Related Articles 1H NMR structure of the heme pocket of HNO-myoglobin. J Biol Inorg Chem. 2003 Feb;8(3):348-52 Authors: Sulc F, Fleischer E, Farmer PJ, Ma D, La Mar GN The unique (1)H NMR signal of nitrosyl hydride at 14.8 ppm is used to obtain a solution structure of the distal pocket of Mb-HNO, a rare nitroxyl adduct with a half-life of several months at room temperature. (1)H NMR, NOESY and TOCSY data were obtained under identical experimental conditions on solutions of the diamagnetic...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate reveal
Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. Related Articles Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J Mol Biol. 2002 Sep 27;322(4):841-9 Authors: Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J The mechanical unfolding of an immunoglobulin domain from the...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] 19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes o
19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant. Related Articles 19F NMR of trifluoroacetyl-labeled cysteine mutants of myoglobin: structural probes of nitric oxide bound to the H93G cavity mutant. Biochemistry. 2001 Jul 24;40(29):8588-96 Authors: Thomas MR, Boxer SG Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine,...
nmrlearner Journal club 0 11-19-2010 08:44 PM
[NMR paper] 1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin
1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin. Related Articles 1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin. Biochim Biophys Acta. 1995 Apr 27;1248(2):149-58 Authors: Yamamoto Y, Suzuki T, Hori H Met-azido and met-imidazole forms of the myoglobin from the mollusc Dolabella auricularia have been studied by 1H-NMR and EPR spectroscopy. In the mollusc myoglobin, in which His-E7 is replaced by Val, the guanidino group of Arg-E10 serves as an alternative hydrogen-bond...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. Eur J Biochem. 1993 Jul 15;215(2):431-7 Authors: Banci L, Bertini I, Marconi S, Pierattelli R The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellu
Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4731-3 Authors: Kreutzer U, Wang DS, Jue T The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl...
nmrlearner Journal club 0 08-21-2010 11:41 PM
(2)H NMR study of the water dynamics in hydrated myoglobin.
(2)H NMR study of the water dynamics in hydrated myoglobin. Related Articles (2)H NMR study of the water dynamics in hydrated myoglobin. J Phys Chem B. 2010 Aug 12;114(31):10209-16 Authors: Lusceac SA, Vogel M We use 1D and 2D (2)H NMR to study the temperature-dependent mechanism for the rotational motion of myoglobin hydration water. The results show that isotropic and anisotropic water reorientation is observed at high and low temperatures, respectively, with a continuous crossover in the temperature range of 200-230 K. The anisotropic...
nmrlearner Journal club 0 08-17-2010 03:36 AM


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 - 2024, 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 10:41 AM.


Map