Collapse Transitions of Proteins and the Interplay among Backbone, Sidechain, and Solvent Interactions

Alex S. Holehouse, Rohit V. Pappu

Research output: Contribution to journalReview articlepeer-review

53 Scopus citations

Abstract

Proteins can collapse into compact globules or form expanded, solvent-accessible, coil-like conformations. Additionally, they can fold into well-defined three-dimensional structures or remain partially or entirely disordered. Recent discoveries have shown that the tendency for proteins to collapse or remain expanded is not intrinsically coupled to their ability to fold. These observations suggest that proteins do not have to form compact globules in aqueous solutions. They can be intrinsically disordered, collapsed, or expanded, and even form well-folded, elongated structures. This ability to decouple collapse from folding is determined by the sequence details of proteins. In this review, we highlight insights gleaned from studies over the past decade. Using a polymer physics framework, we explain how the interplay among sidechains, backbone units, and solvent determines the driving forces for collapsed versus expanded states in aqueous solvents.

Original languageEnglish
Pages (from-to)19-39
Number of pages21
JournalAnnual Review of Biophysics
Volume47
DOIs
StatePublished - May 20 2018

Keywords

  • collapse
  • intrinsically disordered proteins
  • polymer physics
  • solvent quality
  • unfolded states

Fingerprint

Dive into the research topics of 'Collapse Transitions of Proteins and the Interplay among Backbone, Sidechain, and Solvent Interactions'. Together they form a unique fingerprint.

Cite this