期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 109, 期 23, 页码 11777-11780出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp045267p
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We have used ion mobility mass spectrometry to study the effect of D-residues on helix formation in unsolvated alanine-based peptides. The right-handed helix of Ac-A(15)K + H+ is significantly disrupted when five or more of the natural L-residues are randomly replaced with D-residues. On the other hand, when a block of L-residues is replaced with D-residues, an unusual ambidextrous structure with helical segments of opposite chirality is formed. A peptide with all D-residues forms a left-handed helix.
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