Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism.

Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Research Abstract Details 

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Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Abstract Text:

J Utsumi,S Yamazaki,K Hosoi,H Shimizu,K Kawaguchi,F Inagaki,

The conformations of fibroblast and E. coli-derived recombinant human interferon-beta s were studied by circular dichroism and nuclear magnetic resonance spectroscopy in the acidic pH region of 4.6 to 1.6. Both interferons have very similar conformations with high alpha-helix contents (approximately 70%). These results suggest that glycosylation does not appreciably change the conformation of human interferon-beta. Moreover, a slow conformational change is observed below pH 2.0, which induces the disruption of beta-sheets.

Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Publishing Authors By Initials

J Utsumi,S Yamazaki,K Hosoi,H Shimizu,K Kawaguchi,F Inagaki,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 99

Page Numbers: 1533-5

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1986

Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: biosynthesis

Chemical & Substance for Abstract: Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism. Information

Substance Name: Recombinant Proteins

Registry Number: 0

Grant and Affiliation Information for Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism.

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Country: JAPAN

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MEDLINETA: J Biochem

REFSOURCE: J Biochem (Tokyo) 1986 Oct;100(4):1107

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