Time, space, and disorder in the expanding proteome universe

David Paul Minde, A. Dunker, Kathryn S. Lilley

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Proteins are highly dynamic entities. Their myriad functions require specific structures, but proteins’ dynamic nature ranges all the way from the local mobility of their amino acid constituents to mobility within and well beyond single cells. A truly comprehensive view of the dynamic structural proteome includes: (i) alternative sequences, (ii) alternative conformations, (iii) alternative interactions with a range of biomolecules, (iv) cellular localizations, (v) alternative behaviors in different cell types. While these aspects have traditionally been explored one protein at a time, we highlight recently emerging global approaches that accelerate comprehensive insights into these facets of the dynamic nature of protein structure. Computational tools that integrate and expand on multiple orthogonal data types promise to enable the transition from a disjointed list of static snapshots to a structurally explicit understanding of the dynamics of cellular mechanisms.

Original languageEnglish (US)
Article number1600399
JournalProteomics
Volume17
Issue number7
DOIs
StatePublished - Apr 1 2017

Fingerprint

Proteome
Proteins
Structural dynamics
Biomolecules
Conformations
Amino Acids

Keywords

  • Alternative splicing
  • Conformation
  • Intrinsically disordered protein
  • Membrane proteins
  • Post-translational modification

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Time, space, and disorder in the expanding proteome universe. / Minde, David Paul; Dunker, A.; Lilley, Kathryn S.

In: Proteomics, Vol. 17, No. 7, 1600399, 01.04.2017.

Research output: Contribution to journalArticle

Minde, David Paul ; Dunker, A. ; Lilley, Kathryn S. / Time, space, and disorder in the expanding proteome universe. In: Proteomics. 2017 ; Vol. 17, No. 7.
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