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Additional resources for Methods of Biochemical Analysis, Volume 28
Over short exchange times and limited pH ranges, the temperature and pH dependence of the rate constant for P(DLA) follows (1). Three empirical equations based on (1) have been proposed for calculation of k&. , 1972) The temperature T is in degrees centigrade. The validity of (4)is, however, limited and exceptions are frequently observed. P(DLA) at greater than two half-lives deviates from first order kinetics at pHgin (Englander and Poulsen, 1969) such that the last 25% of the hydrogens exchange at least twofold times more slowly than do the first 75%.
2. Random-Coil Homopolypeptides The random-coil homopolypeptides, especially poly(D,L-alanine), have traditionally served as models for the hydrogen exchange characteristics of a protein peptide group when the group has full exposure to solvent. Some relevant data for three random-coil homopolypeptides are shown in Table 111. For P(DLA) extension of the backbone relative 52 ALFRED D. Od pH meter reading. ' ( 1 ) Molday et al. (1972);(2) Bryan and Nielsen (1960):(3)Englander and Poulsen (1969): I' (4) Englander et al.
T h e polymer backbone is constructed frotn alkyl groups while the amide resides in the side chain. We have assembled, in Table 1 1 , the ACQUISITION AND INTERPRETATION OF HYDROGEN EXCHANGE DATA 47 available data on the hydrogen exchange properties of the polymer amides and of their constituent monomers or analogs. Both the polymers and monomers exhibit first order hydrogen exchange over at least four half-lives. , 1971; Miller and Klotz, 1973) data were taken over only 1 to 2 pH units, so that deviations from (1) at pH values well removed from pH,,i, would not be detected.
Methods of Biochemical Analysis, Volume 28