%0 Journal Article %1 jelinek_nmr_1997 %A Jelinek, R %A Terry, T D %A Gesell, J J %A Malik, P %A Perham, R N %A Opella, S J %D 1997 %J J. Mol. Biol. %K Capsid,Cloning,Crystallography,Epitopes,HIV Conformation,X-Ray Envelope Fragments,Peptide Library,Protein Protein Resonance Spectroscopy,Models,Molecular,Neutralization Tests,Peptide gp120,HIV-1,Inovirus,Magnetic %N 4 %P 649--655 %R 10.1006/jmbi.1996.0821 %T \NMR\ structure of the principal neutralizing determinant of \HIV\-1 displayed in filamentous bacteriophage coat protein %V 266 %X An NMR approach for structure determination of short peptides displayed on the surface of filamentous bacteriophage virions is demonstrated using the hexapeptide GPGRAF that constitutes the principal neutralizing determinant of HIV-1. This peptide was inserted near the N terminus of the major coat protein of bacteriophage fd. NMR studies of the recombinant protein solubilized in detergent micelles showed that the inserted peptide adopts a double bend S-shaped conformation that is similar to the antibody-bound structure determined by X-ray crystallography. This indicates that a peptide displayed on the bacteriophage coat protein has an enhanced propensity to adopt a conformation similar to that found in the native protein from which it is derived. This approach may be generally applicable to the structure determination of peptide epitopes and other small peptides.

@article{jelinek_nmr_1997, abstract = {An NMR approach for structure determination of short peptides displayed on the surface of filamentous bacteriophage virions is demonstrated using the hexapeptide GPGRAF that constitutes the principal neutralizing determinant of HIV-1. This peptide was inserted near the N terminus of the major coat protein of bacteriophage fd. NMR studies of the recombinant protein solubilized in detergent micelles showed that the inserted peptide adopts a double bend S-shaped conformation that is similar to the antibody-bound structure determined by X-ray crystallography. This indicates that a peptide displayed on the bacteriophage coat protein has an enhanced propensity to adopt a conformation similar to that found in the native protein from which it is derived. This approach may be generally applicable to the structure determination of peptide epitopes and other small peptides.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Jelinek, R and Terry, T D and Gesell, J J and Malik, P and Perham, R N and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/275774ec2d1bb4b99b869539823b5d72a/nmrresource}, doi = {10.1006/jmbi.1996.0821}, interhash = {716b2babff42c75547243128eba637df}, intrahash = {75774ec2d1bb4b99b869539823b5d72a}, issn = {0022-2836}, journal = {J. Mol. Biol.}, keywords = {Capsid,Cloning,Crystallography,Epitopes,HIV Conformation,X-Ray Envelope Fragments,Peptide Library,Protein Protein Resonance Spectroscopy,Models,Molecular,Neutralization Tests,Peptide gp120,HIV-1,Inovirus,Magnetic}, month = mar, number = 4, pages = {649--655}, pmid = {9102458}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{{\{}NMR{\}} structure of the principal neutralizing determinant of {\{}HIV{\}}-1 displayed in filamentous bacteriophage coat protein}}, volume = 266, year = 1997 }