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 02-02-2011, 02:40 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,178
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 Residual interactions in unfolded bile acid-binding protein by (19) F NMR.

Residual interactions in unfolded bile acid-binding protein by (19) F NMR.

Residual interactions in unfolded bile acid-binding protein by (19) F NMR.

Protein Sci. 2011 Feb;20(2):327-35

Authors: Basehore HK, Ropson IJ

The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak assignments were made by site-specific 4FPhe incorporation. The resonances for proteins specifically labeled at Phe17, Phe47, and Phe63 showed changes in chemical shift at denaturant concentrations at which the remaining five phenylalanine residues appear to be fully solvent-exposed. Phe17 is a helical residue that was not expected to participate in a folding initiation site. Phe47 and Phe63 form part of a hydrophobic core region that may be conserved as a site for folding initiation in the intracellular lipid-binding protein family.

PMID: 21280124 [PubMed - in process]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR. Related Articles Residual interactions in unfolded bile acid-binding protein by (19)F-NMR. Protein Sci. 2010 Nov 29; Authors: Basehore HK, Ropson IJ The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19)F-NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak assignments...
nmrlearner Journal club 0 12-01-2010 04:41 PM
[NMR paper] NMR studies of protein-nucleic acid interactions.
NMR studies of protein-nucleic acid interactions. Related Articles NMR studies of protein-nucleic acid interactions. Methods Mol Biol. 2004;278:289-312 Authors: Varani G, Chen Y, Leeper TC Protein-DNA and protein-RNA complexes play key functional roles in every living organism. Therefore, the elucidation of their structure and dynamics is an important goal of structural and molecular biology. Nuclear magnetic resonance (NMR) studies of protein and nucleic acid complexes have common features with studies of protein-protein complexes: the...
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] Probing residual interactions in unfolded protein states using NMR spin relaxation te
Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta. Related Articles Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta. J Am Chem Soc. 2003 Oct 1;125(39):11988-92 Authors: Choy WY, Kay LE Residual interactions in delta131delta, a large disordered fragment of staphylococcal nuclease, have been probed at two different pHs using backbone (15)N and side-chain methyl (2)H NMR spin relaxation...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[NMR paper] NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobi
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Related Articles NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry. 2001 Mar 27;40(12):3561-71 Authors: Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ Apomyoglobin forms a denatured state under low-salt conditions at pH 2.3. The conformational propensities and polypeptide backbone dynamics...
nmrlearner Journal club 0 11-19-2010 08:32 PM
[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure. J Biol Chem. 2001 Mar 9;276(10):7291-301 Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C ...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Biochemistry. 1997 Feb 25;36(8):2278-90 Authors: Hodsdon ME, Cistola DP The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange. Biochemistry. 1997 Feb 25;36(8):2278-90 Authors: Hodsdon ME, Cistola DP The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
nmrlearner Journal club 0 08-22-2010 03:03 PM
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
Theoretical framework for NMR residual dipolar couplings in unfolded proteins O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov Journal of Biomolecular NMR; 2007; 39(1) pp 1-16 Abstract: A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...
stewart Journal club 0 08-05-2008 02:26 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 05:44 PM.


Map