Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.
about
Exciton circular dichroism couplet arising from nitrile-derivatized aromatic residues as a structural probe of proteins.Optimization of a β-sheet-cap for long loop closure.A pH Switch for β-Sheet Protein Folding.Hairpin structure stability plays a role in the activity of two antimicrobial peptides.Biological consequences of improving the structural stability of hairpins that have antimicrobial activity.
P2860
Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.
description
2016 nî lūn-bûn
@nan
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
2016年论文
@zh
2016年论文
@zh-cn
name
Aryl-Aryl interactions in desi ...... timal structure stabilization.
@en
type
label
Aryl-Aryl interactions in desi ...... timal structure stabilization.
@en
prefLabel
Aryl-Aryl interactions in desi ...... timal structure stabilization.
@en
P2093
P2860
P356
P1433
P1476
Aryl-aryl interactions in desi ...... nt for structure stabilization
@en
P2093
Aimee Byrne
Brandon L Kier
Brice Jurban
Jordan M Anderson
Lisa A Eidenschink
Mike Hudson
Niels H Andersen
R M Fesinmeyer
P2860
P304
P356
10.1002/BIP.22821
P577
2016-06-01T00:00:00Z