Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57. | Zendy

Goutam Das | Zendy; David R. Hickey | Zendy; D. McLendon | Zendy; George McLendon | Zendy; Fred Sherman | Zendy

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Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57.

Author(s) -

Goutam Das,

David R. Hickey,

D. McLendon,

George McLendon,

Fred Sherman

Publication year - 1989

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.86.2.496

Subject(s) - saccharomyces cerevisiae , asparagine , mutagenesis , chemistry , yeast , isoleucine , mutant , biochemistry , site directed mutagenesis , cytochrome , cytochrome c , directed mutagenesis , stereochemistry , leucine , enzyme , amino acid , gene , mitochondrion

Two Saccharomyces cerevisiae yeast mutants, cyc1-73 and cyc1-190, contain nonfunctional and presumably unstable forms of iso-1-cytochrome c due to Gly-34----Ser and His-38----Pro replacements, respectively. Second-site reversions that produced Asn-57----Ile replacements at least partially restored function, presumably by alleviating the instability of these two altered iso-1-cytochromes c. Introduction of the Ile-57 replacement by site-directed mutagenesis in an otherwise normal protein resulted in a 17 degrees C increase in the transition temperature (Tm), corresponding to over a 2-fold increase in the free energy change (delta G degrees) for thermal unfolding.

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