Long proteins with unique optimal foldings in the H-P model

DOI10.1016/S0925-7721(02)00134-7zbMath1019.92012MaRDI QIDQ1873159

David Bremner, Erik D. Demaine, Michael Soss, Henk G. Meijer, Oswin Aichholzer, Vera Sacristán

Publication date: 19 May 2003

Published in: Computational Geometry (Search for Journal in Brave)

zbMATH Keywords

energyminimizationcombinatorial geometryprotein foldingfolding stabilityhydrophobic-hydrophilic model

Mathematics Subject Classification ID

Applications of graph theory (05C90) Biochemistry, molecular biology (92C40) Biophysics (92C05)

Related Items

Long proteins with unique optimal foldings in the H-P model ⋮ An integer programming model for protein structure prediction using the 3D-HP side chain model ⋮ Stochastic protein folding simulation in the three-dimensional HP-model

Cites Work

• Finding the lowest free energy conformation of a protein is an NP-hard problem: Proof and implications
• Long proteins with unique optimal foldings in the H-P model
• Optimization in computational chemistry and molecular biology. Local and global approaches. Conference, Princeton Univ., Princeton, NJ, USA, May 7--9, 1999
• On the number of trees in Z^d
• Molecular Modeling of Proteins and Mathematical Prediction of Protein Structure
• Enumerations of lattice animals and trees
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