Left-handed and ambidextrous helices in the gas phase

Article Abstract:

The effect of D-residues on helix formation in unsolvated alanine-based peptides is studied with ion mobility mass spectrometry. It states that when L-residues are replaced with D-residues an unusual ambidextrous structure with helical segments of opposite chirality is formed and D-residues form a left-handed helix.

Analytical Laboratory Instrument Manufacturing, Analytical instruments, Ion Mass Spectroscopy, Analysis, Mass spectrometry, Alanine

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Disrupting helix formation in unsolved peptides

Article Abstract:

Studies of helix disruption caused by inserting a block of glycine residues into a polyalanine peptide are described. According to molecular dynamics simulations, the glycines do not cause a localized disruption of the helices, as might be expected for a residue considered a helix breaker.

Basic Chemical Manufacturing, Industrial Organic Chemicals, Organic Chemicals, Organic compounds

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Metal ion interactions with polyalanine peptides

Article Abstract:

Electrospray mass spectrometry and ion mobility measurements have been used to perform a systematic study of complex formation between metal ions and polyalanine peptides. Several metals studied here have important roles in biological systems.

Spectrum analysis, Spectroscopy, Chemical reactions, Metal ions

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