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Title: Spectroscopic investigation of structure in octarellin (a denovo protein designed to adopt the alpha-beta-barrel packing)
Authors: Beauregard, M ×
Goraj, K
Goffin, V
Heremans, Karel
Goormaghtigh, E
Ruysschaert, Jm
Martial, Ja #
Issue Date: Jan-1991
Publisher: Oxford univ press united kingdom
Series Title: Protein engineering vol:4 issue:7 pages:745-749
Abstract: We present here a spectroscopic structural characterization of octarellin, a recently reported de novo protein modelled on alpha/beta-barrel proteins [K. Goraj, A. Renard and J.A. Martial (1990) Protein Engng, 3, 259-2661. Infrared and Raman spectra analyses of octarellin's secondary structure reveal the expected percentage of alpha-helices (30%) and a higher beta-sheet content (40%) than predicted from the design. When the Raman spectra obtained with octarellin and native triose-phosphate isomerase (a natural alpha/beta-barrel) are compared, similar percentages of secondary structures are found. Thermal denaturation of octarellin monitored by CD confirms that its secondary structures are quite stable, whereas its native-like tertiary fold is not. Tyrosine residues, predicted to be partially hidden from solvent, are actually exposed as revealed by Raman and UV absorption spectra. We conclude that the attempted alpha/beta-barrel conformation in octarellin may be loosely packed. The criteria used to design octarellin are discussed and improvements suggested.
ISSN: 0269-2139
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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