Geometry of proteins: hydrogen bonding, sterics, and marginally compact tubes
The functionality of proteins is governed by their structure in the native state. Protein structures are made up of emergent building blocks of helices and almost planar sheets. A simple coarse-grained geometrical model of a flexible tube barely subject to compaction provides a unified framework for...
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| Published in | Physical review. E, Statistical, nonlinear, and soft matter physics Vol. 73; no. 3 Pt 1; p. 031921 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
01.03.2006
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| Subjects | |
| Online Access | Get more information |
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| Abstract | The functionality of proteins is governed by their structure in the native state. Protein structures are made up of emergent building blocks of helices and almost planar sheets. A simple coarse-grained geometrical model of a flexible tube barely subject to compaction provides a unified framework for understanding the common character of globular proteins. We argue that a recent critique of the tube idea is not well founded. |
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| AbstractList | The functionality of proteins is governed by their structure in the native state. Protein structures are made up of emergent building blocks of helices and almost planar sheets. A simple coarse-grained geometrical model of a flexible tube barely subject to compaction provides a unified framework for understanding the common character of globular proteins. We argue that a recent critique of the tube idea is not well founded. |
| Author | Maritan, Amos Trovato, Antonio Seno, Flavio Banavar, Jayanth R Lezon, Timothy Cieplak, Marek Marenduzzo, Davide Kamien, Randall D Flammini, Alessandro Snir, Yehuda Hoang, Trinh X |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16605572$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_physa_2007_04_075 crossref_primary_10_1039_C9SM00851A crossref_primary_10_1016_j_gene_2008_06_004 crossref_primary_10_1002_prot_26567 crossref_primary_10_1007_s10659_014_9472_7 crossref_primary_10_1103_PhysRevE_74_051918 crossref_primary_10_1080_07391102_2009_10507284 crossref_primary_10_1039_C6SM00542J crossref_primary_10_1088_1751_8113_45_22_225208 crossref_primary_10_1103_PhysRevE_75_051114 crossref_primary_10_1039_C2SM26967H crossref_primary_10_1098_rsif_2008_0085 crossref_primary_10_1103_PhysRevLett_99_178104 |
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| SubjectTerms | Computer Simulation Hydrogen Bonding Models, Chemical Models, Molecular Nanotubes - chemistry Nanotubes - ultrastructure Protein Conformation Proteins - chemistry Proteins - ultrastructure Stereoisomerism |
| Title | Geometry of proteins: hydrogen bonding, sterics, and marginally compact tubes |
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