Invariant Tryptophan at a Shielded Site Promotes Folding of the Conformational Unit of Spectrin

The tryptophan that is highly conserved among repeating structural units of spectrin is reported to promote the conformational stability of one such unit of chicken brain α-spectrin. Four constructs were inserted into pET vectors for overexpression in Escherichia coli of the following spectrin pepti...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1994-02, Vol.91 (4), p.1299-1303
Hauptverfasser:	MacDonald, Ruby I., Musacchio, Andrea, Holmgren, Robert A., Saraste, Matti
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Animals Biochemistry Biological and medical sciences Brain Chemistry Chickens Chymotrypsin - metabolism Circular Dichroism Conserved Sequence DNA Mutational Analysis Escherichia coli - genetics Fluorescence Fundamental and applied biological sciences. Psychology Glycoproteins Light scattering Molecular Sequence Data Molecular spectra Molecular weight Pancreatic Elastase - metabolism Peptide Fragments - chemistry Peptide Fragments - metabolism Phosphates Protein Folding Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Scattering, Radiation Sodium Spectrin - chemistry Spectrin - genetics Spectrin - metabolism Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Tryptophan - chemistry Tryptophan - genetics Ultraviolet Rays Ungulates Wavelengths
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