Publications
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Author Title Type [ Year] Filters: Keyword is Models and Author is Jeffrey Skolnick [Clear All Filters]
Pages
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.
Protein fragment reconstruction using various modeling techniquesJournal of Computer-Aided Molecular Design 17, 725–38, 2003.
A simple lattice model that exhibits a protein-like cooperative all-or-none folding transitionBiopolymers 69, 399–405, 2003.
TOUCHSTONE II: a new approach to ab initio protein structure predictionBiophysical Journal 85, 1145–64, 2003.
Unfolding of globular proteins: monte carlo dynamics of a realistic reduced modelBiophysical Journal 85, 3271–3278, 2003.
Ab initio protein structure prediction on a genomic scale: application to the Mycoplasma genitalium genomeProceedings of the National Academy of Sciences of the United States of America 99, 5993–5998, 2002.
Computer simulations of protein folding with a small number of distance restraintsActa Biochimica Polonica 49, 683–692, 2002.
Numerical study of the entropy loss of dimerization and the folding thermodynamics of the GCN4 leucine zipperBiophysical Journal 83, 2801–2811, 2002.
TOUCHSTONE: an ab initio protein structure prediction method that uses threading-based tertiary restraintsProceedings of the National Academy of Sciences of the United States of America 98, 10125–30, 2001.
Ab initio folding of proteins using restraints derived from evolutionary informationProteins Suppl. 3, 177–185, 1999.
Dynamics and thermodynamics of beta-hairpin assembly: insights from various simulation techniquesBiophysical Journal 77, 2942–52, 1999.
Assembly of protein structure from sparse experimental data: an efficient Monte Carlo modelProteins 32, 475–494, 1998.
Fold assembly of small proteins using monte carlo simulations driven by restraints derived from multiple sequence alignmentsJournal of Molecular Biology 277, 419–448, 1998.
Nativelike topology assembly of small proteins using predicted restraints in Monte Carlo folding simulationsProceedings of the National Academy of Sciences of the United States of America 95, 1020–1025, 1998.
MONSSTER: a method for folding globular proteins with a small number of distance restraintsJournal of Molecular Biology 265, 217–241, 1997.
Does a backwardly read protein sequence have a unique native state?Protein Engineering 9, 5–14, 1996.
On the origin of the cooperativity of protein folding: implications from model simulationsProteins 26, 271–287, 1996.
Are proteins ideal mixtures of amino acids? Analysis of energy parameter setsProtein Science: a Publication of the Protein Society 4, 2107–2117, 1995.