activity
19922026
most citedStudies of an Off-Lattice Model for Protein Folding: Sequence Dependence and Improved Sampling at Finite Temperature

124 citations · 971 across the 28 of their papers we have counts for

collaborators

28 papers

physics.geo-ph2026

Joint Bayesian inference of Earth's magnetic field and core surface flow on millennial timescales

Andreas Nilsson, Neil Suttie, Marie Troyano +3

Understanding Earth's core dynamics over millennial timescales requires models that jointly describe the evolution of the geomagnetic field and core surface flow, while accommodati…

quant-ph2025

Designing lattice proteins with variational quantum algorithms

Hanna Linn, Lucas Knuthson, Anders Irbäck +3

Quantum heuristics have shown promise in solving various optimization problems, including lattice protein folding. Equally relevant is the inverse problem, protein design, where on…

quant-ph2024★ 22 cited

Using quantum annealing to design lattice proteins

Anders Irbäck, Lucas Knuthson, Sandipan Mohanty +1

Quantum annealing has shown promise for finding solutions to difficult optimization problems, including protein folding. Recently, we used the D-Wave Advantage quantum annealer to…

quant-ph2022

Folding lattice proteins with quantum annealing

Anders Irbäck, Lucas Knuthson, Sandipan Mohanty +1

Quantum annealing is a promising approach for obtaining good approximate solutions to difficult optimization problems. Folding a protein sequence into its minimum-energy structure…

physics.bio-ph2018★ 6 cited

Markov modeling of peptide folding in the presence of protein crowders

Daniel Nilsson, Sandipan Mohanty, Anders Irbäck

We use Markov state models (MSMs) to analyze the dynamics of a -hairpin-forming peptide in Monte Carlo (MC) simulations with interacting protein crowders, for two different type…

physics.bio-ph2016★ 13 cited

Thermodynamics of amyloid formation and the role of intersheet interactions

Anders Irbäck, Jonas Wessén

The self-assembly of proteins into -sheet-rich amyloid fibrils has been observed to occur with sigmoidal kinetics, indicating that the system initially is trapped in a metastabl…

q-bio.BM2013★ 16 cited

Mechanical resistance in unstructured proteins

S. Æ. Jónsson, S. Mitternacht, A. Irbäck

Single-molecule pulling experiments on unstructured proteins linked to neurodegenerative diseases have measured rupture forces comparable to those for stable folded proteins. To in…

cond-mat.stat-mech2009★ 18 cited

Unfolding times for proteins in a force clamp

Stefano Luccioli, Alberto Imparato, Simon Mitternacht +2

The escape process from the native valley for proteins subjected to a constant stretching force is examined using a model for a Beta-barrel. For a wide range of forces, the unfoldi…

cond-mat.soft2001★ 101 cited

Monte Carlo Update for Chain Molecules: Biased Gaussian Steps in Torsional Space

Giorgio Favrin, Anders Irbäck, Fredrik Sjunnesson

We develop a new elementary move for simulations of polymer chains in torsion angle space. The method is flexible and easy to implement. Tentative updates are drawn from a (conform…

cond-mat.soft2000★ 106 cited

Three-helix-bundle Protein in a Ramachandran Model

Anders Irbäck, Fredrik Sjunnesson, Stefan Wallin

We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and fi…

cond-mat.soft2000★ 58 cited

On Hydrophobicity Correlations in Protein Chains

Anders Irbäck, Erik Sandelin

We study the statistical properties of hydrophobic/polar model sequences with unique native states on the square lattice. It is shown that this ensemble of sequences differs from r…

cond-mat.soft1998★ 54 cited

Monte Carlo Study of the Phase Structure of Compact Polymer Chains

Anders Irbäck, Erik Sandelin

We study the phase behavior of single homopolymers in a simple hydrophobic/hydrophilic off-lattice model with sequence independent local interactions. The specific heat is, not une…

cond-mat.soft1998

Design of Sequences with Good Folding Properties in Coarse-Grained Protein Models

Anders Irbäck, Carsten Peterson, Frank Potthast +1

Background: Designing amino acid sequences that are stable in a given target structure amounts to maximizing a conditional probability. A straightforward approach to accomplish thi…

cond-mat.soft1997★ 29 cited

Monte Carlo Procedure for Protein Design

Anders Irbäck, Carsten Peterson, Frank Potthast +1

A new method for sequence optimization in protein models is presented. The approach, which has inherited its basic philosophy from recent work by Deutsch and Kurosky [Phys. Rev. Le…

cond-mat.soft1997★ 32 cited

Local Interactions and Protein Folding: A Model Study on the Square and Triangular Lattices

Anders Irbäck, Erik Sandelin

We study a simple heteropolymer model containing sequence-independent local interactions on both square and triangular lattices. Sticking to a two-letter code, we investigate the m…

physics.chem-ph1996★ 104 cited

Local Interactions and Protein Folding: A 3D Off-Lattice Approach

Anders Irbäck, Carsten Peterson, Frank Potthast +1

The thermodynamic behavior of a three-dimensional off-lattice model for protein folding is probed. The model has only two types of residues, hydrophobic and hydrophilic. In absence…

chem-ph1996★ 57 cited

Identification of Amino Acid Sequences with Good Folding Properties in an Off-Lattice Model

Anders Irbäck, Carsten Peterson, Frank Potthast

Folding properties of a two-dimensional toy protein model containing only two amino-acid types, hydrophobic and hydrophilic, respectively, are analyzed. An efficient Monte Carlo pr…

adap-org1996

Comment on `Avalanche Dynamics in Evolution, Growth and Depinning Models'

Mats Dahlbom, Anders Irbäck

This paper is withdrawn.

chem-ph1996

Binary Assignments of Amino Acids from Pattern Conservation

Anders Irbäck, Frank Potthast

We develop a simple optimization procedure for assigning binary values to the amino acids. The binary values are determined by a maximization of the degree of pattern conservation…

chem-ph1995★ 98 cited

Evidence for Non-Random Hydrophobicity Structures in Protein Chains

Anders Irbäck, Carsten Peterson, Frank Potthast

The question of whether proteins originate from random sequences of amino acids is addressed. A statistical analysis is performed in terms of blocked and random walk values formed…

chem-ph1995

Sequence Dependence in an Off-Lattice Model for Protein Folding

Anders Irbäck, Frank Potthast

See chem-ph/9505003.

chem-ph1995★ 124 cited

Studies of an Off-Lattice Model for Protein Folding: Sequence Dependence and Improved Sampling at Finite Temperature

Anders Irbäck, Frank Potthast

We study the thermodynamic behavior of a simple off-lattice model for protein folding. The model is two-dimensional and has two different ``amino acids''. Using numerical simulatio…

hep-lat1993★ 32 cited

Hybrid Monte Carlo simulation of polymer chains

A. Irbäck

We develop the hybrid Monte Carlo method for simulations of single off-lattice polymer chains. We discuss implementation and choice of simulation parameters in some detail. The per…

hep-lat1993★ 13 cited

Scaling in Steiner Random Surfaces

C. F. Baillie, A. Irback, W. Janke +1

It has been suggested that the modified Steiner action functional has desirable properties for a random surface action. In this paper we investigate the scaling of the string tensi…