Impact of chemical heterogeneity on protein self-assembly in water
DC Field | Value | Language |
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dc.contributor.author | Chong, Song-Ho | - |
dc.contributor.author | Ham, Sihyun | - |
dc.date.available | 2021-02-22T12:46:24Z | - |
dc.date.issued | 2012-05 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.issn | 1091-6490 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/11904 | - |
dc.description.abstract | Hydrophobicity is thought to underlie self-assembly in biological systems. However, the protein surface comprises hydrophobic and hydrophilic patches, and understanding the impact of such a chemical heterogeneity on protein self-assembly in water is of fundamental interest. Here, we report structural and thermodynamic investigations on the dimer formation of full-length amyloid-beta proteins in water associated with Alzheimer's disease. Spontaneous dimerization process-from the individual diffusive regime at large separations, through the approach stage in which two proteins come close to each other, to the structural adjustment stage toward compact dimer formation-was captured in full atomic detail via unguided, explicit-water molecular dynamics simulations. The integral-equation theory of liquids was then applied to simulated protein structures to analyze hydration thermodynamic properties and the water-mediated interaction between proteins. We demonstrate that hydrophilic residues play a key role in initiating the dimerization process. A long-range hydration force of enthalpic origin acting on the hydrophilic residues provides the major thermodynamic force that drives two proteins to approach from a large separation to a contact distance. After two proteins make atomic contacts, the nature of the water-mediated interaction switches from a long-range enthalpic attraction to a short-range entropic one. The latter acts both on the hydrophobic and hydrophilic residues. Along with the direct protein-protein interactions that lead to the formation of intermonomer hydrogen bonds and van der Waals contacts, the water-mediated attraction of entropic origin brings about structural adjustment of constituent monomer proteins toward the formation of a compact dimer structure. | - |
dc.format.extent | 6 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | Impact of chemical heterogeneity on protein self-assembly in water | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1073/pnas.1120646109 | - |
dc.identifier.scopusid | 2-s2.0-84861217855 | - |
dc.identifier.wosid | 000304369800024 | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.109, no.20, pp 7636 - 7641 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 109 | - |
dc.citation.number | 20 | - |
dc.citation.startPage | 7636 | - |
dc.citation.endPage | 7641 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | MOLECULAR-DYNAMICS SIMULATIONS | - |
dc.subject.keywordPlus | BETA-DIMER FORMATION | - |
dc.subject.keywordPlus | HYDROPHOBIC HYDRATION | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | COLLAPSE | - |
dc.subject.keywordPlus | AGGREGATION | - |
dc.subject.keywordPlus | CONFINEMENT | - |
dc.subject.keywordPlus | DEPENDENCE | - |
dc.subject.keywordPlus | SOLVATION | - |
dc.subject.keywordPlus | CHEMISTRY | - |
dc.subject.keywordAuthor | solvation thermodynamics | - |
dc.subject.keywordAuthor | dehydration | - |
dc.subject.keywordAuthor | protein interface | - |
dc.identifier.url | https://www.pnas.org/content/109/20/7636 | - |
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