Research Topics
Species | Iskra StanevaSummaryAffiliation: Lund University Country: Sweden Publications
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Detail Information
Publications
All-atom Monte Carlo approach to protein-peptide bindingIskra Staneva
Computational Biology and Biological Physics, Department of Theoretical Physics, Lund University, Solvegatan 14 A, SE 223 62 Lund, Sweden
J Mol Biol 393:1118-28. 2009..This is done in particular for a set of related sequences binding to the third PDZ domain of PSD-95 with encouraging results...
Monte Carlo study of the formation and conformational properties of dimers of Aβ42 variantsSimon Mitternacht
Computational Biology and Biological Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
J Mol Biol 410:357-67. 2011..Our findings hint at reorganization of this part of the molecule as a potentially critical step in Aβ aggregation...
Binding free energy landscape of domain-peptide interactionsIskra Staneva
Department of Astronomy and Theoretical Physics, Computational Biology and Biological Physics Group, Lund University, Lund, Sweden
PLoS Comput Biol 7:e1002131. 2011..Our combined results are consistent with a binding mechanism in which the peptide C terminal residue binds in an initial, rate-limiting step...
Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics studyIskra Staneva
Department of Astronomy and Theoretical Physics, Computational Biology and Biological Physics Group, Lund University, Lund, Sweden
PLoS Comput Biol 8:e1002682. 2012..Our results highlight the importance of overall physical properties of IDP segments, such as net charge or presence of strongly hydrophobic amino acids, for molecular recognition via coupled folding-binding...
Comparing the folding free-energy landscapes of Abeta42 variants with different aggregation propertiesSimon Mitternacht
Computational Biology and Biological Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
Proteins 78:2600-8. 2010..Comparing results for the four Abeta42 variants, we identify specific conformational properties of residues 23-26 that might play a key role in aggregation...
