Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.
about
Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.How quickly can a β-hairpin fold from its transition state?Light-Switchable Peptides with a Hemithioindigo Unit: Peptide Design, Photochromism, and Optical Spectroscopy.Directly monitor protein rearrangement on a nanosecond-to-millisecond time-scale.
P2860
Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Infrared study of the stabilit ...... tides with a common NPDG turn.
@ast
Infrared study of the stabilit ...... tides with a common NPDG turn.
@en
Infrared study of the stabilit ...... tides with a common NPDG turn.
@nl
type
label
Infrared study of the stabilit ...... tides with a common NPDG turn.
@ast
Infrared study of the stabilit ...... tides with a common NPDG turn.
@en
Infrared study of the stabilit ...... tides with a common NPDG turn.
@nl
prefLabel
Infrared study of the stabilit ...... tides with a common NPDG turn.
@ast
Infrared study of the stabilit ...... tides with a common NPDG turn.
@en
Infrared study of the stabilit ...... tides with a common NPDG turn.
@nl
P2093
P2860
P356
P1476
Infrared study of the stabilit ...... tides with a common NPDG turn.
@en
P2093
P2860
P304
15332-15338
P356
10.1021/JP2046867
P407
P577
2011-12-02T00:00:00Z