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Spontaneous aggregation of fibril-forming peptides studied by molecular dynamics simulations.
Authors: Matthes, D.
Name of University: Georg-August-Universität Göttingen
Place of University: Göttingen
Date of Approval (YYYY-MM-DD): 2011-12-08
Document Type: PhD-Thesis
ID: 576430.0
Mapping the conformational dynamics and pathways of spontaneous steric zipper peptide oligomerization.
Authors: Matthes, D.; Gapsys, V.; Daebel, V.; de Groot, B. L.
Date of Publication (YYYY-MM-DD): 2011-05-03
Title of Journal: PLoS ONE
Volume: 6
Issue / Number: 5
Sequence Number of Article: e19129
Document Type: Article
ID: 563623.0
Secondary structure propensities in peptide folding simulations: A systematic comparison of molecular mechanics interaction schemes.
Authors: Matthes, D.; de Groot, B. L.
Date of Publication (YYYY-MM-DD): 2009-07-22
Title of Journal: Biophysical Journal
Volume: 97
Issue / Number: 2
Start Page: 599
End Page: 608
Document Type: Article
ID: 433416.0
Primary steps of pH-dependent insulin aggregation kinetics are governed by conformational flexibility.
Authors: Haas, J.; Voehringer-Martinez, E.; Boegehold, A.; Matthes, D.; Hensen, U.; Pelah, A.; Abel, B.; Grubmueller, H.
Date of Publication (YYYY-MM-DD): 2009-07-20
Title of Journal: ChemBioChem
Volume: 10
Issue / Number: 11
Start Page: 1816
End Page: 1822
Document Type: Article
ID: 432075.0
Entries: 1-4  
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