Using a combination of one- and two-dimensional methods, 1H- and 15N-nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic undecapeptide CTTTNSRGTTT in DMSO solution. Nuclear Over-hauser enhancement spectroscopy experiments indicated the presence of secondary structures, mainly turn-like structures, which only represent a family, albeit a dominant one, of an ensemble of conformations available to the peptide. Since reverse turns may play an important role as intermediates in protein folding, the experimental observations described here may link the immunological and theoretical approaches to protein folding
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, d...
grantor: University of TorontoThe isolated N-terminal SH3 domain of the Drosophila signali...
Drosocin is a cationic 19 amino acid peptide secreted by Drosophila in response to septic injury. Th...
Using a combination of one- and two-dimensional methods, H-1- and N-15-nmr spectroscopy has been emp...
International audienceRabies virus glycoprotein (G) is a trimeric type I transmembrane glycoprotein ...
It is generally accepted that protein folding proceeds via local folded intermediates which functio...
Structural characterization of several peptides and a protein was done over a wide range of detail b...
The conformational properties of a 21-residue peptide, corresponding to amino acids 255 to 275 (F255...
The means by which a polypeptide chain acquires its unique 3-D structure is a fundamental question i...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
Successful protein folding is central to all biological cellular processes with a large portion of t...
It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G,...
This thesis describes the use of nuclear magnetic resonance techniques to determine the structures o...
It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G ...
Two proposed glycosylation sites are located within T cell epitopes of rabies virus glycoprotein, na...
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, d...
grantor: University of TorontoThe isolated N-terminal SH3 domain of the Drosophila signali...
Drosocin is a cationic 19 amino acid peptide secreted by Drosophila in response to septic injury. Th...
Using a combination of one- and two-dimensional methods, H-1- and N-15-nmr spectroscopy has been emp...
International audienceRabies virus glycoprotein (G) is a trimeric type I transmembrane glycoprotein ...
It is generally accepted that protein folding proceeds via local folded intermediates which functio...
Structural characterization of several peptides and a protein was done over a wide range of detail b...
The conformational properties of a 21-residue peptide, corresponding to amino acids 255 to 275 (F255...
The means by which a polypeptide chain acquires its unique 3-D structure is a fundamental question i...
AbstractNMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding,...
Successful protein folding is central to all biological cellular processes with a large portion of t...
It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G,...
This thesis describes the use of nuclear magnetic resonance techniques to determine the structures o...
It has recently been reported that synthetic peptides corresponding to the C-terminal sequence of G ...
Two proposed glycosylation sites are located within T cell epitopes of rabies virus glycoprotein, na...
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, d...
grantor: University of TorontoThe isolated N-terminal SH3 domain of the Drosophila signali...
Drosocin is a cationic 19 amino acid peptide secreted by Drosophila in response to septic injury. Th...