The physics of protein self-assembly
| dc.contributor.author | McManus, JJ | |
| dc.contributor.author | Charbonneau, P | |
| dc.contributor.author | Zaccarelli, E | |
| dc.contributor.author | Asherie, N | |
| dc.date.accessioned | 2017-08-23T15:40:48Z | |
| dc.date.available | 2017-08-23T15:40:48Z | |
| dc.date.issued | 2016-04-01 | |
| dc.description.abstract | © 2016 The Authors. Understanding protein self-assembly is important for many biological and industrial processes. Proteins can self-assemble into crystals, filaments, gels, and other amorphous aggregates. The final forms include virus capsids and condensed phases associated with diseases such as amyloid fibrils. Although seemingly different, these assemblies all originate from fundamental protein interactions and are driven by similar thermodynamic and kinetic factors. Here we review recent advances in understan ding protein self-assembly through a soft condensed matter perspective with an emphasis on three specific systems: globular proteins, viruses, and amyloid fibrils. We conclude with a discussion of unanswered questions in the field. | |
| dc.identifier.eissn | 1879-0399 | |
| dc.identifier.issn | 1359-0294 | |
| dc.identifier.uri | ||
| dc.publisher | Elsevier BV | |
| dc.relation.ispartof | Current Opinion in Colloid and Interface Science | |
| dc.relation.isversionof | 10.1016/j.cocis.2016.02.011 | |
| dc.title | The physics of protein self-assembly | |
| dc.type | Journal article | |
| duke.contributor.orcid | Charbonneau, P|0000-0001-7174-0821 | |
| pubs.begin-page | 73 | |
| pubs.end-page | 79 | |
| pubs.organisational-group | Chemistry | |
| pubs.organisational-group | Duke | |
| pubs.organisational-group | Physics | |
| pubs.organisational-group | Trinity College of Arts & Sciences | |
| pubs.publication-status | Published | |
| pubs.volume | 22 |