Electronic circular dichroism and nuclear magnetic resonance studies of peptides derived from the FKBP52‐interacting β‐turn of the hERα ligand‐binding domain-Reference-Cited by-同舟云学术

Electronic circular dichroism and nuclear magnetic resonance studies of peptides derived from the FKBP52‐interacting β‐turn of the hERα ligand‐binding domain

Published:2019-01-25 Issue:4 Volume:111 Page:
ISSN:2475-8817
Container-title:Peptide Science
language:en
Short-container-title:Peptide Science

Author:

Byrne Cillian¹²,Belnou Mathilde¹,Baulieu Etienne‐Emile²,Lequin Olivier¹,Jacquot Yves¹^ORCID

Affiliation:

1. Sorbonne Université, Ecole Normale SupérieurePSL University, CNRS UMR 7203, Laboratoire des Biomolécules Paris France

2. Institut Baulieu, Université Paris‐SaclayINSERM UMR 1195, Neuroprotection and Neuroregeneration Le Kremlin Bicêtre France

Funder

Fondation française de gérontologie

Institut Baulieu

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pep2.24113

Reference105 articles.

1. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units

2. β-turns in proteins

3. Turns in Peptides and Proteins

4. Roles of β-turns in protein folding: From peptide models to protein engineering

5. Synthesis, conformational properties, and antibody recognition of peptides containing .beta.-turn mimetics based on .alpha.-alkylproline derivatives

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