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
Home Forums Wiki NMR feeds Downloads Register Today's Posts



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  
Old 11-19-2010, 08:32 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,734
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 NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

Related Articles NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

Biochemistry. 2001 May 8;40(18):5414-21

Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR

The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.

PMID: 11331005 [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
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine Ce?dric Laguri, Nicolas Sapay, Jean-Pierre Simorre, Bernhard Brutscher, Anne Imberty, Pierre Gans and Hugues Lortat-Jacob http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201753e/aop/images/medium/ja-2011-01753e_0006.gif Journal of the American Chemical Society DOI: 10.1021/ja201753e http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
nmrlearner Journal club 0 06-09-2011 01:32 AM
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine. 13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine. J Am Chem Soc. 2011 Jun 2; Authors: Laguri C, Sapay N, Simorre JP, Brutscher B, Imberty A, Gans P, Lortat-Jacob H Heparan sulfate, a polysaccharide of the glycosaminoglycan family characterized by a unique level of complexity, has emerged as a key...
nmrlearner Journal club 0 06-04-2011 11:26 AM
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5.
Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5. Solution NMR Structure of apo-calmodulin in complex with the IQ motif of Human Cardiac Sodium Channel Na(V)1.5. J Mol Biol. 2010 Dec 14; Authors: Chagot B, Chazin WJ The function of the human voltage-gated sodium channel Na(V)1.5 is regulated in part by intracellular calcium signals. The ubiquitous calcium sensor protein calmodulin (CaM) is an important part of the complex calcium-sensing apparatus in Na(V)1.5. CaM interacts with an IQ...
nmrlearner Journal club 0 12-21-2010 01:00 PM
[NMR paper] NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migrat
NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. Related Articles NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. J Biol Chem. 2003 Jun 6;278(23):21212-20 Authors: Fan D, Zheng Y, Yang D, Wang J We report here the NMR structure and backbone dynamics of an exchangeable apolipoprotein, apoLp-III, from the insect Locusta migratoria. The NMR structure adopts an up-and-down elongated five-helix bundle, which is similar to the...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] NMR structure and dynamics of a receptor-active apolipoprotein E peptide.
NMR structure and dynamics of a receptor-active apolipoprotein E peptide. Related Articles NMR structure and dynamics of a receptor-active apolipoprotein E peptide. J Biol Chem. 2002 Aug 9;277(32):29172-80 Authors: Raussens V, Slupsky CM, Ryan RO, Sykes BD Apolipoprotein E (apoE) is important in lipid metabolism due to its interaction with members of the low density lipoprotein (LDL) receptor family. ApoE is able to interact with the LDL receptor only when it is bound to lipid particles. To address structural aspects of this phenomenon, a...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Biochemistry. 1997 Nov 4;36(44):13657-66 Authors: Wang G, Sparrow JT, Cushley RJ The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR. Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR. Biochemistry. 1994 Nov 8;33(44):12990-7 Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS...
nmrlearner Journal club 0 08-22-2010 03:29 AM
[NMR paper] Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl
Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy. Related Articles Interaction of apocytochrome c and derived polypeptide fragments with sodium dodecyl sulfate micelles monitored by photochemically induced dynamic nuclear polarization 1H NMR and fluorescence spectroscopy. Biochemistry. 1991 Apr 9;30(14):3387-95 Authors: Snel MM, Kaptein R, de Kruijff B The topology of apocytochrome c, the...
nmrlearner Journal club 0 08-21-2010 11:16 PM



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 10:01 PM.


Map