The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design
about
Insights from molecular dynamics simulations for computational protein design.Designed α-sheet peptides suppress amyloid formation in Staphylococcus aureus biofilms.Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins.Unfavorable regions in the ramachandran plot: Is it really steric hindrance? The interacting quantum atoms perspective.Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins.
P2860
The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design
description
2016 nî lūn-bûn
@nan
2016 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
The effect of chirality and st ...... ties: tools for protein design
@ast
The effect of chirality and st ...... ties: tools for protein design
@en
type
label
The effect of chirality and st ...... ties: tools for protein design
@ast
The effect of chirality and st ...... ties: tools for protein design
@en
prefLabel
The effect of chirality and st ...... ties: tools for protein design
@ast
The effect of chirality and st ...... ties: tools for protein design
@en
P2860
P50
P356
P1476
The effect of chirality and st ...... ties: tools for protein design
@en
P2860
P304
P356
10.1093/PROTEIN/GZW023
P577
2016-06-09T00:00:00Z