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Effects of incorporation of azido moieties into the hydrophobic core of coiled coil peptidesElectronic supplementary information (ESI) available: General peptide synthesis, procedures for CD measurements including spectra, DLS, TEM, FT-IR, and SEM measurements, confocal microscopy measurements including labelling of L4Z4 aggregates with FITC. See DOI: 10.1039/c4cc09089f
The secondary structure of the coiled coil peptides was regulated by altering the azido content at the hydrophobic core. These peptides were further investigated to form higher-order assemblies presumably via azido-mediated interactions. Controlled peptide folding via the variation of azido content.
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creator | Cheong, Jian Liang Lim, Jaehong Toh, Jerry K. C Jee, Joo-Eun Wong, Lan Li Venkataraman, Shrinivas Lee, Su Seong Lee, Song-Gil |
description | The secondary structure of the coiled coil peptides was regulated by altering the azido content at the hydrophobic core. These peptides were further investigated to form higher-order assemblies presumably
via
azido-mediated interactions.
Controlled peptide folding
via
the variation of azido content. |
doi_str_mv | 10.1039/c4cc09089f |
format | article |
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via
azido-mediated interactions.
Controlled peptide folding
via
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source | Royal Society of Chemistry:Jisc Collections:Royal Society of Chemistry Read and Publish 2022-2024 (reading list) |
title | Effects of incorporation of azido moieties into the hydrophobic core of coiled coil peptidesElectronic supplementary information (ESI) available: General peptide synthesis, procedures for CD measurements including spectra, DLS, TEM, FT-IR, and SEM measurements, confocal microscopy measurements including labelling of L4Z4 aggregates with FITC. See DOI: 10.1039/c4cc09089f |
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