Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4

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

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)48-52
Number of pages5
JournalJournal of Biochemistry and Molecular Biology
Volume31
Issue number1
Publication statusPublished - 1998 Jan 31

Fingerprint

Cyclin-Dependent Kinase Inhibitor p16
Tumor Suppressor Proteins
Circular Dichroism
Conformations
Tumors
Magnetic Resonance Spectroscopy
Peptides
Growth
Structural properties
Catalyst activity
Neoplasms
Proteins
Monomers
Nuclear magnetic resonance

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Lee, Weontae ; Jang, Ji Uk ; Kim, Dong Myeong ; Son, Hosun ; Yang, Beom Seok. / Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4. In: Journal of Biochemistry and Molecular Biology. 1998 ; Vol. 31, No. 1. pp. 48-52.
@article{395b7f8d5f2b48f1bb392ffaf783d9f7,
title = "Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4",
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.",
author = "Weontae Lee and Jang, {Ji Uk} and Kim, {Dong Myeong} and Hosun Son and Yang, {Beom Seok}",
year = "1998",
month = "1",
day = "31",
language = "English",
volume = "31",
pages = "48--52",
journal = "BMB Reports",
issn = "1976-6696",
publisher = "The Biochemical Society of the Republic of Korea",
number = "1",

}

Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4. / Lee, Weontae; Jang, Ji Uk; Kim, Dong Myeong; Son, Hosun; Yang, Beom Seok.

In: Journal of Biochemistry and Molecular Biology, Vol. 31, No. 1, 31.01.1998, p. 48-52.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Overexpression and spectroscopic characterization of a recombinant human tumor suppressor p16INK4

AU - Lee, Weontae

AU - Jang, Ji Uk

AU - Kim, Dong Myeong

AU - Son, Hosun

AU - Yang, Beom Seok

PY - 1998/1/31

Y1 - 1998/1/31

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0032338432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032338432&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0032338432

VL - 31

SP - 48

EP - 52

JO - BMB Reports

JF - BMB Reports

SN - 1976-6696

IS - 1

ER -