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Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationAn Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Secondary structure propensities in peptide folding simulations: a systematic comparison of molecular mechanics interaction schemes.Driving forces and structural determinants of steric zipper peptide oligomer formation elucidated by atomistic simulations.Spontaneous aggregation of the insulin-derived steric zipper peptide VEALYL results in different aggregation forms with common featuresPrimary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility
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description
onderzoeker
@nl
researcher ORCID ID = 0000-0003-3969-6335
@en
name
Dirk Matthes
@ast
Dirk Matthes
@en
Dirk Matthes
@es
Dirk Matthes
@nl
type
label
Dirk Matthes
@ast
Dirk Matthes
@en
Dirk Matthes
@es
Dirk Matthes
@nl
prefLabel
Dirk Matthes
@ast
Dirk Matthes
@en
Dirk Matthes
@es
Dirk Matthes
@nl
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34868371900
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0000-0003-3969-6335