Effects of Hofmeister ions on the α-helical structure of proteins.
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How cations change peptide structure.Hydration of guanidinium depends on its local environment.Covalent dye attachment influences the dynamics and conformational properties of flexible peptides.Conformational free-energy landscapes for a peptide in saline environmentsScorpion toxins prefer salt solutions.Salt effects on hydrophobic-core formation in folding of a helical miniprotein studied by molecular dynamics simulations.Ion-induced alterations of the local hydration environment elucidate Hofmeister effect in a simple classical model of Trp-cage miniprotein.Improved 68 Ga-labeling method using ethanol addition: Application to the α-helical peptide DOTA-FAMP.Divalent magnesium cation concentrations determine the formation of tofu-like precipitates with differing urea solubilities
P2860
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P2860
Effects of Hofmeister ions on the α-helical structure of proteins.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Effects of Hofmeister ions on the α-helical structure of proteins.
@en
type
label
Effects of Hofmeister ions on the α-helical structure of proteins.
@en
prefLabel
Effects of Hofmeister ions on the α-helical structure of proteins.
@en
P2093
P2860
P1433
P1476
Effects of Hofmeister ions on the α-helical structure of proteins
@en
P2093
Joachim Dzubiella
Nikolaus Naredi-Rainer
Roland Wedlich-Söldner
P2860
P304
P356
10.1016/J.BPJ.2012.01.035
P407
P577
2012-02-21T00:00:00Z