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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
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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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2001
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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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
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