Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine-Reference-Cited by-同舟云学术

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Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine

Published:2010 Issue:4 Volume:8 Page:788
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Alías Miriam,Ayuso-Tejedor Sara,Fernández-Recio Juan,Cativiela Carlos,Sancho Javier

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2010/OB/B919671D

Reference35 articles.

1. Screening for peptide drugs from the natural repertoire of biodiverse protein folds

2. Phage display-derived peptides as therapeutic alternatives to antibodies

3. Effective combinatorial strategy to increase affinity of carbohydrate binding by peptides

4. Therapeutic peptides: technological advances driving peptides into development

5. Contemporary strategies for the stabilization of peptides in the α-helical conformation

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2. Short peptides based on the conserved regions of MIEN1 protein exhibit anticancer activity by targeting the MIEN1 signaling pathway;Journal of Biological Chemistry;2024-03

3. Accurate structures and spectroscopic parameters of α,α-dialkylated α-amino acids in the gas-phase: a joint venture of DFT and wave-function composite methods;Physical Chemistry Chemical Physics;2023

4. Effects of chirality and side chain length in C_α,α-dialkylated residues on β-hairpin peptide folded structure and stability;Organic & Biomolecular Chemistry;2023

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