Secondary structure of T4 gene 33 protein. Fourier transform infrared and circular dichroic spectroscopic studies.
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.
Shao
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Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0343, USA.
Kearns
D R
DR
Sanders
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GM
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
D046911:Macromolecular Substances; D014764:Viral Proteins; C085859:gene 33 protein, Enterobacteria phage T4