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Effect of phenyl ring position in the Cα-methylated α-amino acid side chain on peptide preferred conformation

1996; Wiley; Volume: 40; Issue: 5 Linguagem: Inglês

10.1002/(sici)1097-0282(1996)40

1097-0282

Claudio Toniolo, Marco Crisma, Fernando Formaggio, A. Polese, Mitsunobu Doi, Takekazu Ishida, E. Mossel, Quirinus B. Broxterman, J. Kamphuis,

RNA and protein synthesis mechanisms

Peptide ScienceVolume 40, Issue 5 p. 523-527 Effect of phenyl ring position in the Cα-methylated α-amino acid side chain on peptide preferred conformation C. Toniolo, Corresponding Author C. Toniolo Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalyBiopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorM. Crisma, M. Crisma Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorF. Formaggio, F. Formaggio Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorA. Polese, A. Polese Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorM. Doi, M. Doi Osaka University of Pharmaceutical Sciences Osaka 569, JapanSearch for more papers by this authorT. Ishida, T. Ishida Osaka University of Pharmaceutical Sciences Osaka 569, JapanSearch for more papers by this authorE. Mossel, E. Mossel DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this authorQ. Broxterman, Q. Broxterman DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this authorJ. Kamphuis, J. Kamphuis DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this author C. Toniolo, Corresponding Author C. Toniolo Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalyBiopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorM. Crisma, M. Crisma Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorF. Formaggio, F. Formaggio Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorA. Polese, A. Polese Biopolymer Research Center, CNR Department of Organic Chemistry University of Padova 35131 Padova, ItalySearch for more papers by this authorM. Doi, M. Doi Osaka University of Pharmaceutical Sciences Osaka 569, JapanSearch for more papers by this authorT. Ishida, T. Ishida Osaka University of Pharmaceutical Sciences Osaka 569, JapanSearch for more papers by this authorE. Mossel, E. Mossel DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this authorQ. Broxterman, Q. Broxterman DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this authorJ. Kamphuis, J. Kamphuis DSM Research Bio-organic Chemistry Section 6160 MD Geleen, The NetherlandsSearch for more papers by this author First published: 1996 https://doi.org/10.1002/(SICI)1097-0282(1996)40:5 3.0.CO;2-ICitations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract The preferred conformations of Cα-methyl phenylglycine, Cα-methyl phenylalanine, and Cα-methyl homophenylalanine residues, as determined in model peptides (including homopeptides) by Fourier transform ir absorption, 1H-nmr, CD, and x-ray diffraction techniques, are compared with the aim of investigating the effect of phenyl ring position in the Cα-methylated amino acid side chain. This study shows that (a) β-turn and 310-helical structures are preferentially adopted by peptides rich in these Cα-methylated, aromatic α-amino acids and (b) turn and helix handedness is critically biased by the position of side-chain branching. © 1997 John Wiley & Sons, Inc. Biopoly 40: 523–527, 1996 Citing Literature Volume40, Issue51996Pages 523-527 RelatedInformation