Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4

Weontae Lee; Ji Uk Jang; Dong Myeong Kim; Hosun Son; Beom Seok Yang

Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16^INK4

Weontae Lee, Ji Uk Jang, Dong Myeong Kim, Hosun Son, Beom Seok Yang

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

Abstract

p16^INK4, which is a 16-kDa polypeptide protein, inhibits the catalytic activity of the CDK4-cyclinD complex to suppress tumor growth. Both unlabeled and isotopelabeled human tumor suppressor p16^INK4 protein were overexpressed and purified to characterize biochemical and structural properties. The purified p16 binds to monomeric GST-CDK4 and exists in a monomer conformation for several weeks at 4°C. The circular dichroism (CD) data indicates that p16 contains high percentage of α-helix and that the helix percentage maximized at pH value of 7.0. One- and two-dimensional nuclear magnetic resonance (NMR) data suggest that purified p16 from our construct has a unique folded conformation under our experimental conditions and exhibits quite stable conformational characteristics.

Original language	English
Pages (from-to)	48-52
Number of pages	5
Journal	Journal of biochemistry and molecular biology
Volume	31
Issue number	1
Publication status	Published - 1998 Jan 31

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

Cite this

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abstract = "p16INK4, which is a 16-kDa polypeptide protein, inhibits the catalytic activity of the CDK4-cyclinD complex to suppress tumor growth. Both unlabeled and isotopelabeled human tumor suppressor p16INK4 protein were overexpressed and purified to characterize biochemical and structural properties. The purified p16 binds to monomeric GST-CDK4 and exists in a monomer conformation for several weeks at 4°C. The circular dichroism (CD) data indicates that p16 contains high percentage of α-helix and that the helix percentage maximized at pH value of 7.0. One- and two-dimensional nuclear magnetic resonance (NMR) data suggest that purified p16 from our construct has a unique folded conformation under our experimental conditions and exhibits quite stable conformational characteristics.",

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year = "1998",

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AU - Lee, Weontae

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AU - Kim, Dong Myeong

AU - Son, Hosun

AU - Yang, Beom Seok

PY - 1998/1/31

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AB - p16INK4, which is a 16-kDa polypeptide protein, inhibits the catalytic activity of the CDK4-cyclinD complex to suppress tumor growth. Both unlabeled and isotopelabeled human tumor suppressor p16INK4 protein were overexpressed and purified to characterize biochemical and structural properties. The purified p16 binds to monomeric GST-CDK4 and exists in a monomer conformation for several weeks at 4°C. The circular dichroism (CD) data indicates that p16 contains high percentage of α-helix and that the helix percentage maximized at pH value of 7.0. One- and two-dimensional nuclear magnetic resonance (NMR) data suggest that purified p16 from our construct has a unique folded conformation under our experimental conditions and exhibits quite stable conformational characteristics.

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Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16^INK4

Abstract

All Science Journal Classification (ASJC) codes

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