Structure and function of ribonuclease.

Deuterium Bonding Versus Hydrogen Bonding

The denaturation of a macromolecule such as a polypeptide is considered in the case where the total number of noncovalent internal bonds broken in the binding process of the chemical agent is only a fraction, αs, of the total number of noncovalent internal bonds involved in its helical native conformation. Starting from a two-parameter (s, σ) model of the helix–random coil transition of polypeptides, the transition temperature is derived as a function of the fraction αs, and of the concentration and the binding constant of the chemical agent. The lower limit of the transition temperature and the corresponding slope of the transition curve are shown to depend on αs. As an illustration, existing data on the partial acid denaturation of the enzymes ribonuclease A and muromidase are analyzed. The resulting average enthalpies of a noncovalent bond in the native ribonuclease A and muromidase are found to be 1.81 kcal/mole and 1.54 kcal/mole, respectively; the corresponding entropies are 5.4 and 4.4 cal/deg./mole, respectively. As a further example, existing data on a partially methylated enzyme ribonuclease A are also considered.

Partial denaturation of macromolecules by chemical agents

Publisher Summary This chapter discusses internal hydrogen bonding in ribonuclease Ribonuclease shows a transition with the increasing temperature The native molecule is folded in a compact form and is held together by covalent bonds and hydrogen bonds In the case of poly-γ-benzyl-L-glutamate, the transition temperature of deuterated ribonuclease in D2O is different from that of hydrogen-containing ribonuclease in H2O The pH-dependence of reversible denaturation provides a means of detecting hydrogen bonds among ionizable side-chain groups The analysis of the pH-dependence of the UV difference spectrum and optical rotation in terms of equilibria between native and denatured forms in different states of ionization shows that two groups in the native molecule in 015 M KC1 have a pK of about 15 As the temperature is raised at a given pH or the pH is lowered at a given temperature, these groups acquire normal ionization properties The chapter discusses the thermally induced transition in ribonuclease

Internal Hydrogen Bonding in Ribonuclease

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Internal Hydrogen Bonding in Ribonuclease