Abstract
Filaments of bacterial flagella are composed of protein subunits, the flagellins, whose molecular weight ranges between 30,000 and 50,000 daltons depending on the bacterial species from which they are obtained. X-ray diffraction patterns ( Astbury et , al. , 1955 ; Burge, 1961; Swanbeck and Forslind, 1964; Champness and Lowy, 1968) and infrared absorption spectra ( Beighton et , al. , 1958 ) of such flagella suggest the presence of α-helix. Recently, the investigation of flagellin structure by polarimetry has provided additional evidence for the presence of α-helix ( Koffler et , al. , 1966 ; Klein et , al. , 1967; 1967a; 1968 ). This paper, is a report on changes in polarimetric parameters that occur when flagellin molecules undergo a transition between the solubilized and polymerized states. These changes appear to result from changes in helical structure as well as changes due to aggregation.
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