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Ribonuclease denaturation, table

In ribonuclease A 13C spin-lattice relaxation of the carbonyl and a and / carbon atoms is slower in the denaturated protein than in the native sample [177]. Apparently, the skeleton of this macromolecule becomes more flexible on denaturation, probably owing to conformational changes. However, the s carbons of lysine in the native protein exhibit relatively large T, values which change only insignificantly on denaturation [177]. This behavior is attributed to a considerable segmental mobility of the lysine side chain (Table 3.17 [177]). [Pg.177]

Table II. Effect of Cosolvents on the Midpoint (Tm) of the Reversible Native Denatured Transition of Ribonuclease A at pH4 2.8°... Table II. Effect of Cosolvents on the Midpoint (Tm) of the Reversible Native Denatured Transition of Ribonuclease A at pH4 2.8°...
See other pages where Ribonuclease denaturation, table is mentioned: [Pg.316]    [Pg.126]    [Pg.279]    [Pg.39]    [Pg.437]    [Pg.11]    [Pg.499]    [Pg.256]    [Pg.380]    [Pg.43]    [Pg.1083]    [Pg.757]    [Pg.275]    [Pg.168]    [Pg.631]    [Pg.234]    [Pg.265]    [Pg.278]   
See also in sourсe #XX -- [ Pg.197 ]



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Ribonuclease denaturation

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