Related ArticlesNMR 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.
[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...
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[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....
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[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...
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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...
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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...
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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...
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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...
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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...