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 08-22-2010, 03:03 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 21,495
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 studies on the flexibility of the poliovirus C3 linear epitope inserted into diff

NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.

Related Articles NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein.

J Biol Chem. 1997 Jan 3;272(1):362-8

Authors: Lecroisey A, Martineau P, Hofnung M, Delepierre M

A set of permissive positions that tolerate insertions/deletions without major deleterious consequences for the binding activity of the protein was previously identified in the maltose-binding protein. The C3 epitope from poliovirus VP1 protein (93DNPASTTNKDK103) was inserted into eight of these positions and two nonpermissive control sites. NMR studies were performed on the MalE protein, the insertion/deletion mutants, and the C3MalE hybrids to selectively determine the flexible regions in these proteins. Comparison of the C3 epitope mobility in the different hybrid proteins indicates that, whatever its insertion site and independently from the specific sequences of its linkers, the epitope is mostly flexible. The vector protein was shown to unfold partially only in the two C3MalE hybrids that correspond to nonpermissive positions. For one of them (insertion at site 339), both sides of the insert are flexible, and at most one side for all the other hybrids. This result correlates with the antigenicity data on the inserted epitope (Martineau, P., Leclerc, C., and Hofnung, M. (1997) Mol. Immunol, in press.

PMID: 8995270 [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] Solid-state NMR spectroscopic studies of an integral membrane protein inserted into a
Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays. Related Articles Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays. J Am Chem Soc. 2004 Aug 11;126(31):9504-5 Authors: Lorigan GA, Dave PC, Tiburu EK, Damodaran K, Abu-Baker S, Karp ES, Gibbons WJ, Minto RE This communication demonstrates for the first time that solid-state NMR spectroscopic studies can be used to investigate aligned...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer diff
Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments. Related Articles Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments. Glycobiology. 2003 Jun;13(6):435-43 Authors: Rinnbauer M, Ernst B, Wagner B, Magnani J, Benie AJ, Peters T A complex between sialyl Lewisx (alpha-D-Neu5Ac-- beta-D-Gal---beta-D-GlcNAc-O-8 COOMe) and E-selectin was studied using saturation transfer difference (STD) nuclear magnetic resonance (NMR) experiments....
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] NMR studies of the backbone flexibility and structure of human growth hormone: a comp
NMR studies of the backbone flexibility and structure of human growth hormone: a comparison of high and low pH conformations. Related Articles NMR studies of the backbone flexibility and structure of human growth hormone: a comparison of high and low pH conformations. J Mol Biol. 2002 May 3;318(3):679-95 Authors: Kasimova MR, Kristensen SM, Howe PW, Christensen T, Matthiesen F, Petersen J, Sørensen HH, Led JJ (15)N NMR relaxation parameters and amide (1)H/(2)H-exchange rates have been used to characterize the structural flexibility of human...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] NMR solution structure of the inserted domain of human leukocyte function associated
NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. Related Articles NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. J Mol Biol. 2000 Feb 4;295(5):1251-64 Authors: Legge GB, Kriwacki RW, Chung J, Hommel U, Ramage P, Case DA, Dyson HJ, Wright PE The interaction between the leukocyte function-associated antigen-1 (LFA-1) and the intercellular adhesion molecule is thought to be mediated primarily via the inserted domain (I-domain) in the alpha-subunit. The...
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] NMR studies on the structure/function correlations of T-cell-epitope analogs from per
NMR studies on the structure/function correlations of T-cell-epitope analogs from pertussis toxin. Related Articles NMR studies on the structure/function correlations of T-cell-epitope analogs from pertussis toxin. Eur J Biochem. 1998 Jun 1;254(2):313-7 Authors: Scarselli M, Esposito G, De Magistris MT, Domenighini M, Rappuoli R, Burroni G, Bernini A, Niccolai N A synthetic tridecapeptide, corresponding to the 30-42 fragment of the S1 subunit of pertussis toxin, has been structurally characterised by using NMR spectroscopy. The molecule...
nmrlearner Journal club 0 11-17-2010 11:06 PM
[NMR paper] NMR studies on the flexibility of nucleoside diphosphate kinase.
NMR studies on the flexibility of nucleoside diphosphate kinase. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR studies on the flexibility of nucleoside diphosphate kinase. Proteins. 1997 Jun;28(2):150-2 Authors: Xu Y, Lecroisey A, Veron M, Delepierre M, Janin J Human NDP kinase B, product of the nm23-H2 gene, binds DNA. It has been suggested that a helix hairpin on the protein surface, part of the nucleotide substrate binding...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into diff
NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein. J Biol Chem. 1997 Jan 3;272(1):362-8 Authors: Lecroisey A, Martineau P, Hofnung M, Delepierre M A set of permissive positions that tolerate...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] NMR studies on the flexibility of nucleoside diphosphate kinase.
NMR studies on the flexibility of nucleoside diphosphate kinase. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles NMR studies on the flexibility of nucleoside diphosphate kinase. Proteins. 1997 Jun;28(2):150-2 Authors: Xu Y, Lecroisey A, Veron M, Delepierre M, Janin J Human NDP kinase B, product of the nm23-H2 gene, binds DNA. It has been suggested that a helix hairpin on the protein surface, part of the nucleotide substrate binding...
nmrlearner Journal club 0 08-22-2010 03:03 PM


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 - 2022, 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 05:20 AM.


Map