dorsal/arxiv
View SchemaImportance of chirality and reduced flexibility of protein side chains: A study with square and tetrahedral lattice models
| Authors | Jinfeng Zhang, Yu Chen, Rong Chen, Jie Liang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0404013 |
| URL | https://arxiv.org/abs/q-bio/0404013 |
| DOI | 10.1063/1.1756573 |
Abstract
In simple models side chains are often represented implicitly (e.g., by spin-states) or simplified as one atom. We study side chain effects using square lattice and tetrahedral lattice models, with explicitly side chains of two atoms. We distinguish effects due to chirality and effects due to side chain flexibilities, since residues in proteins are L-residues, and their side chains adopt different rotameric states. Short chains are enumerated exhaustively. For long chains, we sample effectively rare events (eg, compact conformations) and obtain complete pictures of ensemble properties of these models at all compactness region. We find that both chirality and reduced side chain flexibility lower the folding entropy significantly for globally compact conformations, suggesting that they are important properties of residues to ensure fast folding and stable native structure. This corresponds well with our finding that natural amino acid residues have reduced effective flexibility, as evidenced by analysis of rotamer libraries and side chain rotatable bonds. We further develop a method calculating the exact side-chain entropy for a given back bone structure. We show that simple rotamer counting often underestimates side chain entropy significantly, and side chain entropy does not always correlate well with main chain packing. Among compact backbones with maximum side chain entropy, helical structures emerges as the dominating configurations. Our results suggest that side chain entropy may be an important factor contributing to the formation of alpha helices for compact conformations.
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"abstract": "In simple models side chains are often represented implicitly (e.g., by\nspin-states) or simplified as one atom. We study side chain effects using\nsquare lattice and tetrahedral lattice models, with explicitly side chains of\ntwo atoms. We distinguish effects due to chirality and effects due to side\nchain flexibilities, since residues in proteins are L-residues, and their side\nchains adopt different rotameric states. Short chains are enumerated\nexhaustively. For long chains, we sample effectively rare events (eg, compact\nconformations) and obtain complete pictures of ensemble properties of these\nmodels at all compactness region. We find that both chirality and reduced side\nchain flexibility lower the folding entropy significantly for globally compact\nconformations, suggesting that they are important properties of residues to\nensure fast folding and stable native structure. This corresponds well with our\nfinding that natural amino acid residues have reduced effective flexibility, as\nevidenced by analysis of rotamer libraries and side chain rotatable bonds. We\nfurther develop a method calculating the exact side-chain entropy for a given\nback bone structure. We show that simple rotamer counting often underestimates\nside chain entropy significantly, and side chain entropy does not always\ncorrelate well with main chain packing. Among compact backbones with maximum\nside chain entropy, helical structures emerges as the dominating\nconfigurations. Our results suggest that side chain entropy may be an important\nfactor contributing to the formation of alpha helices for compact\nconformations.",
"arxiv_id": "q-bio/0404013",
"authors": [
"Jinfeng Zhang",
"Yu Chen",
"Rong Chen",
"Jie Liang"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1063/1.1756573",
"title": "Importance of chirality and reduced flexibility of protein side chains: A study with square and tetrahedral lattice models",
"url": "https://arxiv.org/abs/q-bio/0404013"
},
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