Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

Michael H. Hecht; Julian M. Sturtevant; Robert T. Sauer

doi:10.1002/prot.340010108

Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

Michael H. Hecht, Julian M. Sturtevant, Robert T. Sauer

Research output: Contribution to journal › Article › peer-review

115 Scopus citations

Abstract

Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.

Original language	English (US)
Pages (from-to)	43-46
Number of pages	4
Journal	Proteins: Structure, Function, and Bioinformatics
Volume	1
Issue number	1
DOIs	https://doi.org/10.1002/prot.340010108
State	Published - Jan 1986
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Structural Biology
Biochemistry

Keywords

calorimetry
helix‐coil
mutant
protein stability

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10.1002/prot.340010108

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abstract = "Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.",

keywords = "calorimetry, helix‐coil, mutant, protein stability",

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year = "1986",

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language = "English (US)",

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pages = "43--46",

journal = "Proteins: Structure, Function, and Bioinformatics",

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T1 - Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

AU - Hecht, Michael H.

AU - Sturtevant, Julian M.

AU - Sauer, Robert T.

PY - 1986/1

Y1 - 1986/1

N2 - Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.

AB - Oligonucleotide‐directed mutagenesis has been used to replace α‐helical glycines in the N‐terminal domain of λ repressor with alanines. Since alanine is a significantly better helix‐forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N‐terminal domain by 3–6°.

KW - calorimetry

KW - helix‐coil

KW - mutant

KW - protein stability

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JO - Proteins: Structure, Function, and Bioinformatics

JF - Proteins: Structure, Function, and Bioinformatics

IS - 1

ER -

Stabilization of λ repressor against thermal denaturation by site‐directed Gly→Ala changes in α‐helix 3

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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