A proline-derived transannular N-cap for nucleation of short α-helical peptides.
about
A novel peptide stapling strategy enables the retention of ring-closing amino acid side chains for the Wnt/β-catenin signalling pathway.Effect of Stapling Architecture on Physiochemical Properties and Cell Permeability of Stapled α-Helical Peptides: A Comparative Study.An in-tether sulfilimine chiral center induces β-turn conformation in short peptides.
P2860
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年学术文章
@wuu
2016年学术文章
@zh
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
2016年學術文章
@zh-hant
name
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@en
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@nl
type
label
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@en
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@nl
prefLabel
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@en
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@nl
P2093
P2860
P356
P1476
A proline-derived transannular N-cap for nucleation of short α-helical peptides.
@en
P2093
Dongyuan Wang
Xiaogang Niu
P2860
P304
P356
10.1039/C6CC04672J
P407
P577
2016-06-30T00:00:00Z