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Does a synthetic peptide containing the leucine‐zipper domain of c‐myb form an α‐helical structure in solution?
Author(s) -
Ebneth Andreas,
Adermann Knut,
Wolfes Heiner
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80205-x
Subject(s) - leucine zipper , circular dichroism , peptide , myb , chemistry , bzip domain , zipper , leucine , basic helix loop helix leucine zipper transcription factors , protein secondary structure , biochemistry , stereochemistry , crystallography , peptide sequence , amino acid , dna binding protein , transcription factor , gene , algorithm , computer science
We have examined a synthetic peptide containing the putative leucine zipper domain of the chicken c‐myb proto‐oncogene using circular dichroism (CD) spectroscopy. The peptide adopts an α‐helical structure only at low temperatures and in the presence 2,2,2‐trifluoroethanol.