Turn and Helical Peptide Handedness Governed Exclusively by Side-Chain Chiral Centers-Reference-Cited by-同舟云学术

Turn and Helical Peptide Handedness Governed Exclusively by Side-Chain Chiral Centers

Published:2005-02-01 Issue:7 Volume:127 Page:2036-2037
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Royo Soledad¹,De Borggraeve Wim M.¹,Peggion Cristina¹,Formaggio Fernando¹,Crisma Marco¹,Jiménez Ana I.¹,Cativiela Carlos¹,Toniolo Claudio¹

Affiliation:

1. Department of Organic Chemistry, ICMA, University of Zaragoza-CSIC, 50009 Zaragoza, Spain, and Institute of Biomolecular Chemistry, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja043116u

Reference22 articles.

1. Conformational Preferences of RNase A C-Peptide Derivatives Containing a Highly Constrained Analogue of Phenylalanine

2. Facile synthesis and highly efficient resolution of a constrained cyclopropane analogue of phenylalanine

3. Cyclopropane Amino Acids That Mimic Twoχ1-Conformations of Phenylalanine

4. N-Acetyl-N‘-methylamide Derivative of (2S,3S)-1-Amino-2,3-diphenylcyclopropanecarboxylic Acid: Theoretical Analysis of the Conformational Impact Produced by the Incorporation of the Second Phenyl Group to the Cyclopropane Analogue of Phenylalanine

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