title: Secondary structure of T4 gene 33 protein. Fourier transform infrared and circular dichroic spectroscopic studies.
abstract: The secondary structure of bacteriophage T4 gene 33 protein (gp33) has been quantitatively examined by using Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy. Resolution enhancement techniques, including Fourier deconvolution and derivative spectroscopy were used to quantitate the spectral information from the amide I bands. The relative areas of these component bands indicate 21% alpha-helix, 25% beta-sheet, 34% turn, 12% random coil and 8% other undefined structures in gp33. An analysis of the CD spectrum of gp33 at the same pH and temperature revealed 19% alpha-helix, 25% beta-sheet, 13% turn and 43% random coil structures. The possible reasons for the discrepancies in estimates of the contributions to the secondary structure from turns and random coils are discussed.
authors.affiliation: Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0343, USA.
authors.forename: W
authors.initials: W
authors.lastname: Shao
authors.forename: D R
authors.initials: DR
authors.lastname: Kearns
authors.forename: G M
authors.initials: GM
authors.lastname: Sanders
mesh_terms: D000595:Amino Acid Sequence; D017122:Bacteriophage T4 / Q000737:chemistry / Q000235:genetics; D002942:Circular Dichroism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D046911:Macromolecular Substances; D014764:Viral Proteins; C085859:gene 33 protein, Enterobacteria phage T4