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Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1

Freund, J. and Kellner, R. and Houthaeve, T. and Kalbitzer, Hans Robert (1994) Stability and proteolytic domains of Nef protein from human immunodeficiency virus (HIV) type 1. European journal of biochemistry: EJB (= the FEBS journal) 221 (2), pp. 811-819.

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Abstract

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 ...

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Item Type:Article
Date:1994
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
8174561PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Electrophoresis, Polyacrylamide GelMESH
Escherichia coli/geneticsMESH
Gene Products, nef/metabolismMESH
HIV Protease/metabolismMESH
HIV-1/geneticsMESH
Histidine/metabolismMESH
HumansMESH
Hydrogen-Ion ConcentrationMESH
Magnetic Resonance SpectroscopyMESH
Molecular Sequence DataMESH
Pancreatic Elastase/metabolismMESH
Protein DenaturationMESH
SolubilityMESH
TemperatureMESH
Trypsin/metabolismMESH
Tyrosine/metabolismMESH
nef Gene Products, Human Immunodeficiency VirusMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:08 Sep 2010 08:23
Last Modified:08 Sep 2010 08:23
Item ID:16507
Owner Only: item control page
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