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Microsecond and nanosecond polyproline II helix formation in aqueous nanodrops measured by mass spectrometry.


ABSTRACT: The 1.5 ?s and <400 ns time constants for the formation of polyproline II helix structures in 21 and 16 residue peptides, respectively, are measured using rapid mixing from theta-glass emitters coupled with mass spectrometry. Results from these studies should serve as useful benchmarks for comparison with computational simulation results.

SUBMITTER: Mortensen DN 

PROVIDER: S-EPMC5226856 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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Microsecond and nanosecond polyproline II helix formation in aqueous nanodrops measured by mass spectrometry.

Mortensen Daniel N DN   Williams Evan R ER  

Chemical communications (Cambridge, England) 20161001 82


The 1.5 μs and <400 ns time constants for the formation of polyproline II helix structures in 21 and 16 residue peptides, respectively, are measured using rapid mixing from theta-glass emitters coupled with mass spectrometry. Results from these studies should serve as useful benchmarks for comparison with computational simulation results. ...[more]

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2005-09-20 | GSE2744 | GEO