Capturing the Dynamics of a Spring-Loaded Protein

Joshua A. Mitchell; Megan L. O'Mara

doi:10.1016/j.str.2017.06.008

Capturing the Dynamics of a Spring-Loaded Protein

Joshua A. Mitchell, Megan L. O'Mara^*

^*Corresponding author for this work

Research output: Contribution to journal › Short survey › peer-review

1 Citation (Scopus)

Abstract

Skp and other holdase chaperones bind unfolded bacterial outer membrane proteins, preventing premature folding until they insert into the membrane. In this issue of Structure, Holdbrook et al. (2017) use a combination of NMR, SAXS, ensemble optimization, and MD simulations to show that the Skp chaperone samples a much wider range of conformations than suggested by its structure alone.

Original language	English
Pages (from-to)	963-964
Number of pages	2
Journal	Structure
Volume	25
Issue number	7
DOIs	https://doi.org/10.1016/j.str.2017.06.008
Publication status	Published - 5 Jul 2017

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title = "Capturing the Dynamics of a Spring-Loaded Protein",

abstract = "Skp and other holdase chaperones bind unfolded bacterial outer membrane proteins, preventing premature folding until they insert into the membrane. In this issue of Structure, Holdbrook et al. (2017) use a combination of NMR, SAXS, ensemble optimization, and MD simulations to show that the Skp chaperone samples a much wider range of conformations than suggested by its structure alone.",

author = "Mitchell, {Joshua A.} and O'Mara, {Megan L.}",

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AB - Skp and other holdase chaperones bind unfolded bacterial outer membrane proteins, preventing premature folding until they insert into the membrane. In this issue of Structure, Holdbrook et al. (2017) use a combination of NMR, SAXS, ensemble optimization, and MD simulations to show that the Skp chaperone samples a much wider range of conformations than suggested by its structure alone.

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JO - Structure

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Capturing the Dynamics of a Spring-Loaded Protein

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