Abstract:
:The HPLC retention behavior of three complete single methionine and methionine sulfoxide replacement sets of two 18-mer model peptides and neuropeptide Y (NPY) were investigated. All peptides were prepared by multiple solid-phase peptide synthesis. Plotting the retention time differences between methionine and methionine sulfoxide analogues vs the position of replacement shows that potentially alpha-helical peptides become helical on binding during reversed-phase high performance liquid chromatography. In the case of an amphipathic alpha-helix, the retention time differences change periodically with a 3-4 repeat pattern, which allow the location of amphipathic helical structures. Replacements in nonamphipathic alpha-helical domains cause local preferential binding areas and lead to sequence-dependent retention time profiles. Methionine replacement studies of NPY suggest an unstructured or extended conformation from Tyr1 to Ala12 connected to a well-defined amphipathic alpha-helix from Pro13 to Arg35. The assignment is confirmed by comparison of nuclear Overhauser effects based two-dimensional 1H-nmr spectroscopy and utilization of the C alpha H shift index method in 50% trifluoroethanol/50% water.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Rothemund S,Krause E,Beyermann M,Bienert M,Sykes BD,Sönnichsen FDdoi
10.1002/(SICI)1097-0282(199608)39:2%3C207::AID-BIPsubject
Has Abstractpub_date
1996-08-01 00:00:00pages
207-19issue
2eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(199608)39:2<207::AID-BIP9>journal_volume
39pub_type
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