Macromolecular crowding induces polypeptide compaction and decreases folding cooperativity

Douglas Tsao, Nikolay Dokholyan

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

A cell's interior is comprised of macromolecules that can occupy up to 40% of its available volume. Such crowded environments can influence the stability of proteins and their rates of reaction. Using discrete molecular dynamics simulations, we investigate how both the size and number of neighboring crowding reagents affect the thermodynamic and folding properties of structurally diverse proteins. We find that crowding induces higher compaction of proteins. We also find that folding becomes less cooperative with the introduction of crowders into the system. The crowders may induce alternative non-native protein conformations, thus creating barriers for protein folding in highly crowded media.

Original languageEnglish (US)
Pages (from-to)3491-3500
Number of pages10
JournalPhysical Chemistry Chemical Physics
Volume12
Issue number14
DOIs
StatePublished - Apr 2 2010

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crowding
polypeptides
folding
Compaction
proteins
Peptides
Proteins
Protein folding
Macromolecules
Conformations
Molecular dynamics
macromolecules
Thermodynamics
reagents
thermodynamic properties
molecular dynamics
Computer simulation
cells
simulation

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

Cite this

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Macromolecular crowding induces polypeptide compaction and decreases folding cooperativity. / Tsao, Douglas; Dokholyan, Nikolay.

In: Physical Chemistry Chemical Physics, Vol. 12, No. 14, 02.04.2010, p. 3491-3500.

Research output: Contribution to journalArticle

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