title: Effects of incorporation of azido moieties into the hydrophobic core of coiled coil peptides.
abstract: 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.
authors: Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos, Singapore 138669. sslee@ibn.a-star.edu.sg sglee@ibn.a-star.edu.sg.
authors: Jian Liang
authors: JL
authors: Cheong
authors: Jaehong
authors: J
authors: Lim
authors: Jerry K C
authors: JK
authors: Toh
authors: Joo-Eun
authors: JE
authors: Jee
authors: Lan Li
authors: LL
authors: Wong
authors: Shrinivas
authors: S
authors: Venkataraman
authors: Su Seong
authors: SS
authors: Lee
authors: Song-Gil
authors: SG
authors: Lee
mesh_terms: D001386:Azides / Q000737:chemistry*; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D001386:Azides; D010455:Peptides