Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.
about
Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.Dimension conversion and scaling of disordered protein chains.Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.
P2860
Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Randomizing the unfolded state ...... tions between unlike residues.
@ast
Randomizing the unfolded state ...... tions between unlike residues.
@en
type
label
Randomizing the unfolded state ...... tions between unlike residues.
@ast
Randomizing the unfolded state ...... tions between unlike residues.
@en
prefLabel
Randomizing the unfolded state ...... tions between unlike residues.
@ast
Randomizing the unfolded state ...... tions between unlike residues.
@en
P2093
P2860
P356
P1476
Randomizing the unfolded state ...... tions between unlike residues.
@en
P2093
Christian Richter
Nina Kubatova
Siobhan E Toal
Verena Linhard
P2860
P304
P356
10.1002/CHEM.201406539
P407
P577
2015-02-26T00:00:00Z