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- Hydrophobic-polar_protein_folding_model abstract "The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. All amino acid types are classified as either hydrophobic (H) or polar (P), and the folding of a protein sequence is defined as a self-avoiding walk in a 2D or 3D lattice. The HP model imitates the hydrophobic effect by assigning a negative (favorable) weight to interactions between adjacent, non-covalently bound H residues. Proteins that have minimum energy are assumed to be in their native state.The HP model can be expressed in both two and three dimensions, generally with square lattices, although triangular lattices have been used as well. It has also been studied on general regular lattices.Randomized search algorithms are often used to tackle the HP folding problem. This includes stochastic, evolutionary algorithms like the Monte Carlo method, genetic algorithms, and ant colony optimization. While no method has been able to calculate the experimentally determined minimum energetic state for long protein sequences, the most advanced methods today are able to come close.Even though the HP model abstracts away many of the details of protein folding, it is still an NP-hard problem on both 2D and 3D lattices.Recently, a Monte Carlo method, named FRESS, was developed and appears to perform well on HP models.".
- Hydrophobic-polar_protein_folding_model wikiPageID "11185249".
- Hydrophobic-polar_protein_folding_model wikiPageLength "3446".
- Hydrophobic-polar_protein_folding_model wikiPageOutDegree "19".
- Hydrophobic-polar_protein_folding_model wikiPageRevisionID "609975693".
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Amino_acid.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Ant_colony_optimization_algorithms.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Category:Protein_structure.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Chemical_polarity.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Evolutionary_algorithm.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Genetic_algorithm.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Hydrophobe.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Hydrophobic_effect.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Lattice_(group).
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Lattice_protein.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Monte_Carlo_method.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink NP-hardness.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Native_state.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Protein_folding.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Protein_structure_prediction.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Self-avoiding_walk.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Square_lattice.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLink Stochastic.
- Hydrophobic-polar_protein_folding_model wikiPageWikiLinkText "Hydrophobic-polar protein folding model".
- Hydrophobic-polar_protein_folding_model wikiPageWikiLinkText "hydrophobic properties".
- Hydrophobic-polar_protein_folding_model subject Category:Protein_structure.
- Hydrophobic-polar_protein_folding_model type Biophysic.
- Hydrophobic-polar_protein_folding_model comment "The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state.".
- Hydrophobic-polar_protein_folding_model label "Hydrophobic-polar protein folding model".
- Hydrophobic-polar_protein_folding_model sameAs Q5955260.
- Hydrophobic-polar_protein_folding_model sameAs m.02r2x3j.
- Hydrophobic-polar_protein_folding_model sameAs Q5955260.
- Hydrophobic-polar_protein_folding_model wasDerivedFrom Hydrophobic-polar_protein_folding_model?oldid=609975693.
- Hydrophobic-polar_protein_folding_model isPrimaryTopicOf Hydrophobic-polar_protein_folding_model.