Sterical Recognition at Helix–Helix Interface of Leu-Aib-Based Polypeptides with and without a GxxxG-Motif-Reference-Cited by-同舟云学术

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Sterical Recognition at Helix–Helix Interface of Leu-Aib-Based Polypeptides with and without a GxxxG-Motif

Published:2019-05-13 Issue:22 Volume:35 Page:7249-7254
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Itagaki Toru¹^ORCID,Uji Hirotaka¹^ORCID,Imai Tomoya²^ORCID,Kimura Shunsaku¹^ORCID

Affiliation:

1. Department of Material Chemistry, Graduate School of Engineering, Kyoto University Kyoto-Daigaku-Katsura, Nishikyo-ku, Kyoto 615-8510, Japan

2. Research Institute for Sustainable Humanosphere, Kyoto University, Gokasho, Uji-shi, Kyoto 611-0011, Japan

Funder

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.9b00620

Reference24 articles.

1. Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking

2. Translocation and Reversible Localization of Signaling Proteins

3. Protein-protein interactions: A review of protein dimer structures

4. Protein-protein interaction analysis for functional characterization of helicases

5. Subunit structure of human erythrocyte glycophorin A

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2. Construction of peptide/plasmid DNA complexes for plant gene transfection via the basic leucine zipper domain;Polymer Journal;2024-03-05

3. Peptide flat-rod formation by precise arrangement among enantiomeric hydrophobic helices;Journal of Colloid and Interface Science;2022-07

4. Assembly of π-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework;Journal of the American Chemical Society;2022-04-07

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