Journal article
Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites
The journal of physical chemistry. B, Vol.114(2), pp.809-816
01/21/2010
DOI: 10.1021/jp9105103
PMCID: PMC2818683
PMID: 20000372
Abstract
Ion mobility-mass spectrometry is used to investigate the structure(s) of a series of model peptide [M + H](+) ions to better understand how intrinsic properties affect structure in low dielectric environments. The influence of peptide length, amino acid sequence, and composition on gas-phase structure is examined for a series of model peptides that have been previously studied in solution. Collision cross sections for the [M + H](+) ions of Ac-(AAKAA)(n)Y-NH(2) (n = 3-6) and Ac-Y(AEAAKA)(n)F-NH(2) (n = 2-5) are reported and correlated with candidate structures generated using molecular modeling techniques. The [M + H](+) ions of the AAKAA peptide series each exhibit a single, dominant ion mobility arrival time distribution (ATD) which correlates to partial helical structures, whereas the [M + H](+) ions of the AEAAKA ion series are composed of ATDs which correlate to charge-solvated globules (i.e., the charge is coordinated or solvated by polar peptide functional groups). These data raise numerous questions concerning intrinsic properties (amino acid sequence and composition as well as charge location) that dictate gas-phase peptide ion structure, which may reflect trends for peptide ion structure in low dielectric environments, such as transmembrane segments.
Details
- Title: Subtitle
- Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites
- Creators
- Janel R McLean - Texas A&M UniversityJohn A McLean - Texas A&M UniversityZhaoxiang Wu - Texas A&M UniversityChristopher Becker - Texas A&M UniversityLisa M Pérez - Texas A&M UniversityC Nick Pace - Texas A&M UniversityJ Martin Scholtz - Texas A&M UniversityDavid H Russell - Texas A&M University
- Resource Type
- Journal article
- Publication Details
- The journal of physical chemistry. B, Vol.114(2), pp.809-816
- DOI
- 10.1021/jp9105103
- PMID
- 20000372
- PMCID
- PMC2818683
- NLM abbreviation
- J Phys Chem B
- ISSN
- 1520-6106
- eISSN
- 1520-5207
- Publisher
- American Chemical Society
- Grant note
- 1 T32 GM065088-01A1 / NIGMS NIH HHS R01 RR019587-01 / NCRR NIH HHS T32 GM065088 / NIGMS NIH HHS 1 R01 RR019587-01 / NCRR NIH HHS R01 RR019587 / NCRR NIH HHS
- Language
- English
- Date published
- 01/21/2010
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984293084402771
Metrics
9 Record Views