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, 02:27 PM
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 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 MBP greatly reduces the encephalitogenicity of the protein. Synthetic peptides analogous to this region of MBP containing glycine and histidine are encephalitogenic if they lack the N-terminal half, residues 69-74. However, if they contain both histidine plus the N-terminal half, encephalitogenicity is abolished, suggesting that an interaction of histidine with an amino acid in the N-terminal half changes the conformation or the properties of the peptide. This was investigated by measuring the 1H-NMR spectra of synthetic peptides analogous to this region of MBP, both containing histidine but with and without the N-terminal half. The major difference in the spectra of the two peptides was the pH dependence of line broadening of the histidine resonances. The histidine C2H and C4H resonances were broadened at intermediate pH values in both peptides. However, sharpening of the lines at high pH showed a different pH dependence in the two peptides. For the longer peptide containing the N-terminal half, the lines did not sharpen until the pH was increased above 10.2, coinciding with the pKa of Lys-74. Acetylation of this peptide caused the pH at which the lines began to sharpen to drop to 8.8. In the shorter peptide, lacking the N-terminal half and Lys-74, the lines also sharpened at pH 8.8. The greater broadening which persisted up above pH 10 for the longer peptide suggests slow exchange between two different conformations or environments of the histidine. One of these could be a conformation in which the deprotonated histidine hydrogen bonds with Lys-74. The Lys side-chain resonances indicated a decrease in rotational freedom above the pKa of histidine, consistent with this conclusion. Although this putative interaction between His and Lys-74 did not appear to have a significant effect on the overall conformation of the peptide, it could result in a reduction in encephalitogenicity by altering the properties of the peptide. This could affect processing and presentation of this determinant by antigen presenting cells.

PMID: 8652624 [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] Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP inte
Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae. Related Articles Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae. Biochem J. 1998 Sep 15;334 ( Pt 3):601-7 Authors: Miller RW, Eady RR, Gormal C, Fairhurst SA, Smith BE Investigation of the interaction of MgADP- and MgATP2- with the Fe protein of Klebsiella pneumoniae nitrogenase by 31P NMR showed that the adenine...
nmrlearner Journal club 0 11-17-2010 11:15 PM
[NMR paper] 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...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[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] Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its c
Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs. Related Articles Proton NMR study on a histone-like protein, HU alpha, from Escherichia coli and its complex with oligo DNAs. Biol Pharm Bull. 1993 May;16(5):437-43 Authors: Shindo H, Kurumizaka H, Furubayashi A, Sakuma C, Matsumoto U, Yanagida A, Goshima N, Kano Y, Imamoto F It was confirmed that the flexible arm region of HU alpha forms an antiparallel beta-sheet and that all of the residues of phenylalanines, together with some of...
nmrlearner Journal club 0 08-21-2010 11:53 PM
[NMR paper] Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the inte
Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the gadolinium(III) bis(m-boroxyphenylamide)diethylenetriaminepentaacetic acid complex with human oxygenated and deoxygenated hemoglobin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Metal complexes as allosteric effectors of human hemoglobin: an NMR study of the interaction of the...
nmrlearner Journal club 0 08-21-2010 04:03 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 09:26 AM.


Map