1981
DOI: 10.1016/0005-2795(81)90189-6
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The secondary structure of ovomucoid and its domains as studied by circular dichroism

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Cited by 40 publications
(19 citation statements)
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“…About half of the tyrosyl residues of the protein are exposed under native conditions, as shown by solvent perturbation difference spectroscopy [17]. Ovomucoid is rich in istructure (46%) compared with h-structure (26%), as studied by circular dichroism [18]. The first five thirddomain sequences reported by Laskowski's group (chicken, turkey, ring-necked pheasant, Japanese quail and chachalaca) have five different residues at the reactive site position, P 1 (Ala, Leu, Met, Lys and Gln, respectively).…”
Section: Primary Structure and Physicochemical Propertiesmentioning
confidence: 99%
“…About half of the tyrosyl residues of the protein are exposed under native conditions, as shown by solvent perturbation difference spectroscopy [17]. Ovomucoid is rich in istructure (46%) compared with h-structure (26%), as studied by circular dichroism [18]. The first five thirddomain sequences reported by Laskowski's group (chicken, turkey, ring-necked pheasant, Japanese quail and chachalaca) have five different residues at the reactive site position, P 1 (Ala, Leu, Met, Lys and Gln, respectively).…”
Section: Primary Structure and Physicochemical Propertiesmentioning
confidence: 99%
“…In order to observe the net changes of the polypeptide chain in ovomucoid, all of the equilibrium CD spectra of ovomucoid were corrected by subtracting the spectra of the carbohydrate moiety ·under the same conditions as for corresponding samples. 8 ) The equilibrium CD spectra of ovomucoid at various temperatures and at 20°C in 6 M guanidine hydrochloride are shown in Fig. 5.…”
Section: Methodsmentioning
confidence: 99%
“…8) In the case of a sample .containing 6 M guanidine hydrochloride,. a reference without protein in the same solution was used as the control.…”
Section: Methodsmentioning
confidence: 99%
“…The carbohydrate moiety consists of three oligosaccharide units bound to protein through asparagine residues (Montgomery and Wu 1963). The polypeptide chain is composed of 26 % a-helix, 46 % b-structure, 10 % b-turns, and 18 % random coil (Watanabe et al 1981). Ovomucoid is highly resistant to heat owing to its high cystine content.…”
Section: Ovomucoidmentioning
confidence: 99%