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PMID: 8293811 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Does a synthetic peptide containing the leucine-zipper domain of c-myb form an alpha-helical structure in solution?

FEBS letters ·Vol. 337 ·No. 3 ·1994-01-17 ·Pages 265-8

Ebneth A, Adermann K, Wolfes H

Abstract

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 alpha-helical structure only at low temperatures and in the presence 2,2,2-trifluoroethanol.

MeSH Terms

Amino Acid Sequence Animals Chickens Circular Dichroism Cold Temperature Humans Leucine Zippers Molecular Sequence Data Peptide Fragments/chemistry Protein Structure, Secondary Proto-Oncogene Mas Proto-Oncogene Proteins/chemistry Proto-Oncogene Proteins c-myb Sequence Homology, Amino Acid Solutions Trifluoroethanol/pharmacology

Chemicals

MAS1 protein, human Peptide Fragments Proto-Oncogene Mas Proto-Oncogene Proteins Proto-Oncogene Proteins c-myb Solutions Trifluoroethanol

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Ebneth A

Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Germany.

Adermann K

Wolfes H

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(94)80205-x

Published

1994-01-17

Pages

265-8

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(94)80205-x View journal details

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Does a synthetic peptide containing the leucine-zipper domain of c-myb form an alpha-helical structure in solution?

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