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A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH_2: spectroscopic evidence for a peptide with significant β-turn character in water and in dimethyl sulfoxide

Imperiali, B. and Fisher, S. L. and Moats, R. A. and Prins, T. J. (1992) A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH_2: spectroscopic evidence for a peptide with significant β-turn character in water and in dimethyl sulfoxide. Journal of the American Chemical Society, 114 (9). pp. 3182-3188. ISSN 0002-7863. http://resolver.caltech.edu/CaltechAUTHORS:20180724-152025356

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Abstract

Several tetrapeptides, Ac-Val-Pro-D-Ser-His-NH_2, in particular, show significant type II β-turn character in water and in dimethyl sulfoxide. Evidence for this turn population is provided by 2D-rotating frame nuclear Overhauser effect (ROESY) spectroscopy, ^1H NMR amide temperature coefficients, and circular dichroism (CD) studies. To further investigate which residues specifically contribute to the integrity of the turn, studies on 10 tetrapeptides, having the general sequence AC-LXaa-Pro-D-Xaa-L-Xaa-NH_2, are described. The results show the effects of sequence variations on the type II β-turn forming propensity of these peptides in solution. Conclusions from these studies indicate that a cooperative effect between a sterically hindered, β-branched amino acid at the (i) position and a small, non-β-branched D-amino acid at the (i+2) position promotes turn formation. Implications for use of these sequences as structural nucleation elements in de novo protein design are discussed.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1021/ja00035a002DOIArticle
https://pubs.acs.org/doi/suppl/10.1021/ja00035a002PublisherSupporting Information
Alternate Title:A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH2: spectroscopic evidence for a peptide with significant .beta.-turn character in water and in dimethyl sulfoxide
Additional Information:© 1992 American Chemical Society. Received September 24, 1991. This work was supported by the Caltech Consortium in Chemistry and Chemical Engineering (founding members: E.I. Du Pont de Nemours & Co., Inc., Eastman Kodak Co., and the Minnesota Mining and Manufacturing Co.) and in part by the National Science Foundation (CHE-9104445). Award of a Department of Education Predoctoral Fellowship to S.L.F., an NSF Predoctoral Fellowship to T.J.P., and a Du Pont Young Faculty Award (1990) to B.I. are also gratefully acknowledged.
Funders:
Funding AgencyGrant Number
Caltech Consortium in Chemistry and Chemical EngineeringUNSPECIFIED
NSFCHE-9104445
Department of EducationUNSPECIFIED
NSF Predoctoral FellowshipUNSPECIFIED
E. I. DuPont de Nemours and Company, Inc.UNSPECIFIED
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Division of Chemistry and Chemical Engineering8458
Record Number:CaltechAUTHORS:20180724-152025356
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20180724-152025356
Official Citation:A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-Xaa-L-Xaa-NH2: spectroscopic evidence for a peptide with significant .beta.-turn character in water and in dimethyl sulfoxide B. Imperiali, R. A. Moats, S. L. Fisher, and T. J. Prins Journal of the American Chemical Society 1992 114 (9), 3182-3188 DOI: 10.1021/ja00035a002
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:88214
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:25 Jul 2018 16:33
Last Modified:25 Jul 2018 16:33

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