The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
about
Structure and enzymatic mechanism of a moonlighting dUTPaseMicrosecond molecular dynamics simulation of guanidinium chloride induced unfolding of ubiquitin.Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.Molecular mechanism of misfolding and aggregation of Aβ(13-23).Physical origins of the high structural stability of CLN025 with only ten residues.Optimization of adiponectin-derived peptides for inhibition of cancer cell growth and signaling.
P2860
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
description
2011 nî lūn-bûn
@nan
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
2011年论文
@zh
2011年论文
@zh-cn
name
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@en
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@nl
type
label
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@en
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@nl
prefLabel
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@en
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@nl
P2093
P2860
P356
P1476
The CLN025 decapeptide retains a β-hairpin conformation in urea and guanidinium chloride.
@en
P2093
Marcus P D Hatfield
Richard F Murphy
Sándor Lovas
P2860
P304
P356
10.1021/JP111076J
P407
P577
2011-04-11T00:00:00Z