ArticleMethods in molecular biology (Clifton, N.J.)2007
Packing regularities in biological structures relate to their dynamics.
Article in Methods in molecular biology (Clifton, N.J.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Computational Ways to Enhance Protein Inhibitor Design.Frontiers in molecular biosciences · 2020Article
- Elastic network models capture the motions apparent within ensembles of RNA structures.RNA (New York, N.Y.) · 2014Article
- A mechanistic stress model of protein evolution accounts for site-specific evolutionary rates and their relationship with packing density and flexibility.BMC evolutionary biology · 2014Article
- Intrinsically disordered regions of p53 family are highly diversified in evolution.Biochimica et biophysica acta · 2013Article
- The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure.F1000 biology reports · 2013Article
- The importance of slow motions for protein functional loops.Physical biology · 2012Article
- Free energies for coarse-grained proteins by integrating multibody statistical contact potentials with entropies from elastic network models.Journal of structural and functional genomics · 2011Article
- MAVENs: motion analysis and visualization of elastic networks and structural ensembles.BMC bioinformatics · 2011Article
- Immunoglobulin Structure Exhibits Control over CDR Motion.Immunome research · 2011Article
- Voronoia: analyzing packing in protein structures.Nucleic acids research · 2009Article
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2 authors.
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Abstract
The high packing density inside proteins leads to certain geometric regularities and also is one of the most important contributors to the high extent of cooperativity manifested by proteins in their cohesive domain motions. The orientations between neighboring nonbonded residues in proteins substantially follow the similar geometric regularities, regardless of whether the residues are on the surface or buried, a direct result of hydrophobicity forces. These orientations are relatively fixed and correspond closely to small deformations from those of the face-centered cubic lattice, which is the way in which identical spheres pack at the highest density. Packing density also is related to the extent of conservation of residues, and we show this relationship for residue packing densities by averaging over a large sample or residue packings. There are three regimes: (1) over a broad range of packing densities the relationship between sequence entropy and inverse packing density is nearly linear, (2) over a limited range of low packing densities the sequence entropy is nearly constant, and (3) at extremely low packing densities the sequence entropy is highly variable. These packing results provide important justification for the simple elastic network models that have been shown for a large number of proteins to represent protein dynamics so successfully, even when the models are extremely coarse grained. Elastic network models for polymeric chains are simple and could be combined with these protein elastic networks to represent partially denatured parts of proteins. Finally, we show results of applications of the elastic network model to study the functional motions of the ribosome, based on its known structure. These results indicate expected correlations among its components for the step-wise processing steps in protein synthesis, and suggest ways to use these elastic network models to develop more detailed mechanisms, an important possibility because most experiments yield only static structures.
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