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M9460701.TXT
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1994-06-25
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Document 0701
DOCN M9460701
TI Stability and proteolytic domains of Nef protein from human
immunodeficiency virus (HIV) type 1.
DT 9408
AU Freund J; Kellner R; Houthaeve T; Kalbitzer HR; Max-Planck-Institute for
Medical Research, Department of; Biophysics, Heidelberg, Germany.
SO Eur J Biochem. 1994 Apr 15;221(2):811-9. Unique Identifier : AIDSLINE
MED/94229079
AB Proteolytic experiments in conjunction with 1H-NMR spectroscopy show
that the Nef (negative factor) protein from human immunodeficiency virus
type 1 probably consists of two main domains, the N-terminal anchor
domain at amino acid positions 2-65 and the C-terminal core domain at
positions 66-206. The N-terminal domain is likely to be located at the
surface of the protein, while the C-terminal domain has a compactly
folded core and is stable in the absence of the anchor domain. It is
conceivable that the core domain represents a functional domain of the
Nef protein, activated after the removal of the membrane anchor by the
human-immunodeficiency-virus protease or cellular proteases. Nef is
stable at pH 5-12 and denatures at 317-322 K. The Nef protein remains in
its native conformation in dimethyl-sulfoxide/water mixtures up to 35%
(by vol.), and in acetonitrile/water up to 14% (by vol.). Nef refolds
spontaneously after denaturation with urea or guanidinium hydrochloride.
The 1H-NMR parameters and pKa values of five of the nine histidine
residues and one of the seven tyrosine residues were determined and were
found in four cases to be typical for residues which are not located in
the interior of the protein.
DE Amino Acid Sequence Electrophoresis, Polyacrylamide Gel Escherichia
coli/GENETICS Gene Products, nef/*CHEMISTRY/GENETICS/METABOLISM
Histidine/METABOLISM Human Hydrogen-Ion Concentration HIV
Protease/METABOLISM HIV-1/*CHEMISTRY/GENETICS Molecular Sequence Data
Nuclear Magnetic Resonance Pancreatopeptidase/METABOLISM Protein
Denaturation Solubility Support, Non-U.S. Gov't Temperature
Trypsin/METABOLISM Tyrosine/METABOLISM JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).