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Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Characterization of Gas-Phase Native(-like) Proteins Using Structures for Lossless Ion Manipulations.

Jung Yun Lee1, Viraj D Gandhi1, Christopher Harrilal1

  • 1Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99354, United States.

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Multipass Structures for Lossless Ion Manipulations (SLIM) enhanced gas-phase protein separation, accurately determining charge-state-dependent structures. This advancement enables new native ion mobility spectrometry applications.

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Area of Science:

  • Analytical Chemistry
  • Biophysical Chemistry
  • Separation Science

Background:

  • Structures for Lossless Ion Manipulations (SLIM) offer high-resolution ion separations in the gas phase.
  • Previous SLIM applications have focused on various molecular classes, but protein analysis requires further development.

Purpose of the Study:

  • To investigate multipass SLIM for separating gas-phase proteins in a near-native state.
  • To analyze charge-state-dependent arrival time distributions and conformational changes in proteins.
  • To validate SLIM-derived collision cross-section (CCS) values against drift tube ion mobility spectrometry (DTIMS).

Main Methods:

  • Utilized multipass SLIM separations for carbonic anhydrase (CA), alcohol dehydrogenase (ADH), and apo-transferrin.
  • Obtained experimental CCS values using calibration curves with Agilent Tune Mix ions.
  • Deconvoluted multipass arrival time distributions (ATDs) into single-pass values for CCS determination.
  • Compared SLIM-derived CCS values with DTIMS measurements.

Main Results:

  • Baseline separation of CA charge states (z=9+ to 11+) achieved with 8-m single-pass SLIM.
  • Improved mobility peak resolution for ADH (z=23+ to 25+) with extended path lengths up to 24-m.
  • Observed transition from unimodal to multimodal CCS distributions for apo-transferrin (z=16+ to 18+).
  • Demonstrated selective isolation of specific charge states (e.g., apo-transferrin z=17+) using 40-m multipass separations.
  • SLIM separations showed minimal impact on protein structure and CCS values.

Conclusions:

  • Multipass SLIM effectively separates gas-phase proteins in a near-native state, resolving charge-state-dependent structures.
  • The technique provides accurate CCS values comparable to DTIMS.
  • SLIM's capability for mobility-selective isolation opens avenues for native ion mobility applications and further SLIM-based manipulations.