Research Topics
Species | Anders IrbäckSummaryAffiliation: Lund University Country: Sweden Publications
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Detail Information
Publications
Thermal versus mechanical unfolding of ubiquitinAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
Proteins 65:759-66. 2006..Their combined simulation results thus enable the authors to predict in detail important differences between the thermal and mechanical unfolding behaviors of ubiquitin...
PROFASI: A Monte Carlo simulation package for protein folding and aggregationAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
J Comput Chem 27:1548-55. 2006..Adding new updates is easy. The code runs fast in both single- and multi-chain applications, as is illustrated by several examples...
Dissecting the mechanical unfolding of ubiquitinAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
Proc Natl Acad Sci U S A 102:13427-32. 2005..This order is the same in two- and three-state events and at the different forces studied. The observed order remains to be verified experimentally but appears physically reasonable...
Folding thermodynamics of peptidesAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden
Biophys J 88:1560-9. 2005..g., Betanova). In other cases (in particular, GB1m2 and GB1m3), the different estimates agree reasonably well, indicating a more two-state-like melting behavior...
Spontaneous beta-barrel formation: an all-atom Monte Carlo study of Abeta16-22 oligomerizationAnders Irbäck
Computational Biology and Biological Physics Group, Department of Theoretical Physics, Lund University, SE 223 62 Lund, Sweden
Proteins 71:207-14. 2008..In one of several runs, we observe the spontaneous formation of a beta-barrel with six antiparallel strands. The beta-barrel stands out as the by far most long-lived aggregate seen in our simulations...
Folding thermodynamics of three beta-sheet peptides: a model studyAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, SE 223 62 Lund, Sweden
Proteins 56:110-6. 2004..The magnitude of this dependence matches well with the results obtained in two different experiments on the beta-hairpin...
An effective all-atom potential for proteinsAnders Irbäck
Computational Biology and Biological Physics, Department of Theoretical Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
PMC Biophys 2:2. 2009..PACS Codes: 87.14.E-, 87.15.A-, 87.15.Cc...
Thermodynamics of alpha- and beta-structure formation in proteinsAnders Irbäck
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden
Biophys J 85:1466-73. 2003..We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the alpha-helix forms faster than the beta-hairpin...
Monte Carlo study of the formation and conformational properties of dimers of A?42 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 A? aggregation...
Changing the mechanical unfolding pathway of FnIII10 by tuning the pulling strengthSimon Mitternacht
Computational Biology and Biological Physics, Department of Theoretical Physics, Lund University, Lund, Sweden
Biophys J 96:429-41. 2009..Two of these correspond to the native and fully unfolded states, respectively, whereas the third one can be associated with the major unfolding intermediates...
Folding of a small helical protein using hydrogen bonds and hydrophobicity forcesGiorgio Favrin
Department of Theoretical Physics, Complex Systems Division, Lund University, Lund, Sweden
Proteins 47:99-105. 2002..8 A from the native structure. The sequence-dependent part of our potential is pairwise additive. Our calculations suggest that fine-tuning this potential by parameter optimization is of limited use...
Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forcesGiorgio Favrin
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden
Biophys J 87:3657-64. 2004..For the six-chain system, the aggregated structures can have many different shapes, but certain particularly stable shapes can be identified...
Two-state folding over a weak free-energy barrierGiorgio Favrin
Complex Systems Division, Department of Theoretical Physics, Lund University, , SE-223 62 Lund, Sweden
Biophys J 85:1457-65. 2003..A simple estimate based on diffusion in a square-well potential predicts the relaxation time within a factor of two...
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...
Sequence-based study of two related proteins with different folding behaviorsGiorgio Favrin
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden
Proteins 54:8-12. 2004....
Mutation-induced fold switching among lattice proteinsChristian Holzgräfe
Computational Biology and Biological Physics, Lund University, Sölvegatan 14A, SE 223 62 Lund, Sweden
J Chem Phys 135:195101. 2011..The thermodynamic stability is correlated with mutational stability and is, on average, markedly reduced at the observed fold switches...
Differences in solution behavior among four semiconductor-binding peptidesSimon Mitternacht
Computational Biology and Biological Physics Group, Department of Theoretical Physics, Lund University, Solvegatan 14A, SE 223 62 Lund, Sweden
J Phys Chem B 111:4355-60. 2007..By also analyzing designed mutants of two of the peptides, an experimental test of this hypothesis is proposed...
Accelerating atomic-level protein simulations by flat-histogram techniquesSigurour A E Jónsson
Computational Biology and Biological Physics, Lund University, Sölvegatan 14A, SE 223 62 Lund, Sweden
J Chem Phys 135:125102. 2011..The frequency of barrier crossing, which is low in conventional canonical simulations, can be increased by turning to a two-step procedure based on the Wang-Landau and multicanonical algorithms...
