Publications
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Author [ Title] Type Year Filters: Keyword is Protein Conformation [Clear All Filters]
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Are proteins ideal mixtures of amino acids? Analysis of energy parameter setsProtein Science: a Publication of the Protein Society 4, 2107–2117, 1995.
Assembly of protein structure from sparse experimental data: an efficient Monte Carlo modelProteins 32, 475–494, 1998.
CABS-NMR–De novo tool for rapid global fold determination from chemical shifts, residual dipolar couplings and sparse methyl-methyl NOEsJournal of c\Computational Chemistry 32, 536–44, 2011.
Comparative modeling without implicit sequence alignmentsBioinformatics (Oxford, England) 23, 2522–7, 2007.
Computer simulations of protein folding with a small number of distance restraintsActa Biochimica Polonica 49, 683–692, 2002.
Conservation of complex knotting and slipknotting patterns in proteins.Proceedings of the National Academy of Sciences of the United States of America 109, E1715-23, 2012.
De novo simulations of the folding thermodynamics of the GCN4 leucine zipperBiophysical Journal 77, 54–69, 1999.
Denatured proteins and early folding intermediates simulated in a reduced conformational spaceActa Biochimica Polonica 53, 131–143, 2006.
Distance matrix-based approach to protein structure predictionJournal of Structural and Functional Genomics 10, 67–81, 2009.
Does a backwardly read protein sequence have a unique native state?Protein Engineering 9, 5–14, 1996.
Dynamics and thermodynamics of beta-hairpin assembly: insights from various simulation techniquesBiophysical Journal 77, 2942–52, 1999.
Folding pathway of the b1 domain of protein G explored by multiscale modelingBiophysical Journal 94, 726–36, 2008.
Folding simulations and computer redesign of protein A three-helix bundle motifsProteins 25, 286–299, 1996.
Generalized protein structure prediction based on combination of fold-recognition with de novo folding and evaluation of modelsProteins 61 Suppl. 7, 84–90, 2005.
A minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native stateBiophysical Journal 84, 1518–26, 2003.
MONSSTER: a method for folding globular proteins with a small number of distance restraintsJournal of Molecular Biology 265, 217–241, 1997.