PMID: 42444Oct 24, 1979

Stability of phage T4 lysozymes. II. Unfolding with guanidinium chloride

Biochimica Et Biophysica Acta
M L Elwell, J A Schellman

Abstract

The denaturation by guanidinium chloride of three phage lysozymes (wild type and two mutants) was investigated. The study of solvent denaturation permitted the investigation of the relative stabilities of the proteins at neutral pH, in contrast to thermal denaturation studies reported earlier which could only be performed in acid pH. The results were interpreted assuming that the free energy of solution of proteins is a linear function of denaturant concentration. Using standard thermodynamic formulas this permits the calculation of the stabilities of the three proteins in the absence of guanidinium chloride. The single point mutation Trp 138 leads to Tyr leads to relatively large changes in stability and the interaction of the protein with guanidinium chloride. The changes associated with the subsequent double mutation, Trp 126 leads to Tyr, Trp 158 leads to Tyr, are much smaller indicating a relatively smooth adjustment of the protein structure to the changed side chains. Models of the structural effects of point mutations are discussed. It is found that the mutation at position 138 does not fit a model in which the effect of a substitution is to introduce an energetic strain in the structure. It does fit a model in which the...Continue Reading

References

Sep 1, 1981·Biopolymers·J A SchellmanM Grutter
Oct 29, 1998·Protein Science : a Publication of the Protein Society·M Jucovic, A R Poteete
Jul 23, 1999·Annals of the New York Academy of Sciences·M Jucovic, A R Poteete

Related Concepts

Thermodynamics
Viral Proteins
Bacteriophages
Fluorescence Spectroscopy
Muramidase
Bacteriophage T4
Denaturation
Guanidine Hydrochloride
Mutant
Leftose

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