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 08-22-2010, 03:01 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,700
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 Interaction of two complementary fragments of the bovine spinal cord myelin basic pro

Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.

Related Articles Interaction of two complementary fragments of the bovine spinal cord myelin basic protein with phosphatidylglycerol bilayers, studied by 2H and 31P NMR spectroscopy.

Biochemistry. 1993 Sep 21;32(37):9709-13

Authors: Hayer-Hartl M, Brophy PJ, Marsh D, Watts A

The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with bilayers of dimyristoylphosphatidylglycerol has been studied by broad line 2H and 31P NMR. The fragments, produced by cleavage at the single tryptophan, consist of an N-terminal portion of molecular mass 12.6 kDa and a C-terminal portion of molecular mass 5.8 kDa. The phosphatidylglycerol lipid was deuterated at all three segments of the glycerol headgroup. The approximately linear dependence of the 2H quadrupole splittings and 31P chemical shift anisotropy on protein/lipid ratio in the complexes indicates that the lipids interacting with the protein fragments were in fast exchange on the NMR time scale (approximately 10(-4)-10(-5) s). The relative gradients of the dependence on protein/lipid ratio of both these parameters decrease with the size of the protein fragment and correlate reasonably well with both the net charge on the protein and the lipid binding stoichiometries in the absence of salt. The results are therefore consistent with a model in which the perturbation of the quadrupole splittings either is determined by the net surface potential or is constant for the different protein fragments. Either possibility is consistent with the reduced activity of the fragments relative to the whole protein.

PMID: 7690591 [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] Investigation of the interaction of myelin basic protein with phospholipid bilayers u
Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy. Related Articles Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy. Chem Phys Lipids. 2004 Nov;132(1):47-54 Authors: Pointer-Keenan CD, Lee DK, Hallok K, Tan A, Zand R, Ramamoorthy A Interaction of bovine myelin basic protein and its constituent charge isomers (C1-C3) with phospholipid bilayers was studied using solid-state NMR experiments on model...
nmrlearner Journal club 0 11-24-2010 10:03 PM
[NMR paper] NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and
NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and its antagonist: structural implications for the MHC II (I-Au)-peptide complex from docking calculations. Related Articles NMR and molecular dynamics studies of an autoimmune myelin basic protein peptide and its antagonist: structural implications for the MHC II (I-Au)-peptide complex from docking calculations. Eur J Biochem. 2004 Aug;271(16):3399-413 Authors: Tzakos AG, Fuchs P, van Nuland NA, Troganis A, Tselios T, Deraos S, Matsoukas J, Gerothanassis IP, Bonvin AM ...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Characterization of the interaction between bovine pancreatic trypsin inhibitor and t
Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR. Related Articles Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR. Biophys Chem. 1998 Apr 20;71(2-3):221-34 Authors: Jolivalt C, Böckmann A, Riès-Kautt M, Ducruix A, Guittet E The interaction between Bovine Pancreatic Trypsin Inhibitor and thiocyanate was studied using NMR spectroscopy following several experimental approaches. The chemical shift variations of the BPTI protons in the...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 inte
Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening. Related Articles Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening. Biochim Biophys Acta. 1996 Mar 7;1293(1):23-30 Authors: Koshy KM, Hashim GA, Boggs JM Residues 69-84 of guinea pig myelin basic protein contain the encephalitogenic determinant for the Lewis rat. Insertion of histidine and glycine at positions 77 and 78 in bovine...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Interaction of myelin basic protein with single bilayers on a solid support: an NMR,
Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study. Related Articles Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study. Biochim Biophys Acta. 1993 Sep 19;1151(2):127-36 Authors: Reinl HM, Bayerl TM The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Comparative studies of the interaction of human and bovine platelet factor 4 with hep
Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes. Related Articles Comparative studies of the interaction of human and bovine platelet factor 4 with heparin using histidine NMR resonances as spectroscopic probes. J Protein Chem. 1993 Jun;12(3):303-9 Authors: Talpas CJ, Lee L The pKa values of His-38 and His-50 of the heparin-binding protein, bovine platelet factor 4, are 5.6 and 6.5, respectively, as determined by 1H NMR spectroscopy. The 1H NMR...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[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
Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation
Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope. Related Articles Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope. Biophys J. 2010 Aug 9;99(4):1247-1255 Authors: Ahmed MA, Bamm VV, Harauz G, Ladizhansky V Myelin basic protein (MBP) maintains the tight multilamellar compaction of the myelin sheath in the central nervous system through peripheral binding of adjacent lipid bilayers of...
nmrlearner Journal club 0 08-18-2010 11:15 AM



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 09:25 AM.


Map