Jan 1, 1976

Kinetics of the disordered chain-to-beta transformation of poly(L-tyrosine) in aqueous solution

Biophysical Chemistry
H E Auer, E Patton

Abstract

The kinetics of the transformation of poly(L-tyrosine) from the disordered chain to the intramolecular beta structure in aqueous solution has been studied. The reaction is induced by an isothermal pH jump and is followed by conventional circular dichroism methods. Upon application of curve-fitting procedures, it is found that the kinetics are poorly represented by a single first-order process, but a two-step sequential first-order equation is adequate. Sharp pH-dependent maxima in the phenomenological rate constants and in the fractional amplitude of the rapid step were found. It is proposed to attribute these phenomena to a transition in initial states which is shown to occur over the same pH range within the domain of the disordered-to-beta transition. No sigmoid transient curves were observed, indicating that no slow nucleation events are discernible in this system. These observations contrast strikingly with the mechanism elaborated for beta formation in (Lys)n [R. Hartman et al., J. Mol. Biol. 90 (1974) 415].

Mentioned in this Paper

Sigmoid Colon
Protein Conformation
Polypeptides
Circular Dichroism, Vibrational
Aqueous solution
Tyrosine
Hydrogen-Ion Concentration
Mathematics
Circular Dichroism

About this Paper

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