Effect of Protonation State on the Stability of Amyloid Oligomers Assembled from TTR(105-115).
about
Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers.Early stages of insulin fibrillogenesis examined with ion mobility mass spectrometry and molecular modelling.Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion Spectroscopy.Precursory signatures of protein folding/unfolding: from time series correlation analysis to atomistic mechanisms.End Capping Alters the Structural Characteristics and Mechanical Properties of Transthyretin (105-115) Amyloid Protofibrils.Initial Steps of Amyloidogenic Peptide Assembly Revealed by Cold-Ion SpectroscopyEffects of End-Terminal Capping on Transthyretin (105–115) Amyloid Protofibrils Using Steered Molecular Dynamics
P2860
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P2860
Effect of Protonation State on the Stability of Amyloid Oligomers Assembled from TTR(105-115).
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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name
Effect of Protonation State on ...... s Assembled from TTR(105-115).
@en
type
label
Effect of Protonation State on ...... s Assembled from TTR(105-115).
@en
prefLabel
Effect of Protonation State on ...... s Assembled from TTR(105-115).
@en
P50
P356
P1476
Effect of Protonation State on ...... s Assembled from TTR(105-115).
@en
P2093
Massimiliano Porrini
P304
P356
10.1021/JZ400372U
P577
2013-03-28T00:00:00Z