About: Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism
Creator	Fischer, D Fischer, W Lam, Y Watts, A Judge, P Mehnert, T Routh, A
source	Medline; PMC
abstract	Vpu from HIV‐1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu(1‐32)) and mutant peptides (Vpu(1‐32)‐W23L, Vpu(1‐32)‐R31V, Vpu(1‐32)‐S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu(1‐32)‐W23L has a considerable flickering pattern in the recordings and longer open times than Vpu(1‐32). Whilst recordings for Vpu(1‐32)‐R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu(1‐32)‐S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu(1‐32)‐W23L indicate Michaelis–Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics. Proteins 2008. © 2007 Wiley‐Liss, Inc.
has issue date	2007-10-01(xsd:dateTime)
bibo:doi	10.1002/prot.21642
bibo:pmid	17910056
has license	no-cc
sha1sum (hex)	99c172d0c1ec01074bcb850440e88adf9f1c54b7
schema:url	https://doi.org/10.1002/prot.21642
resource representing a document's title	Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism
has PubMed Central identifier	PMC7167847
has PubMed identifier	17910056
schema:publication	Proteins
resource representing a document's body	covid:99c172d0c1ec01074bcb850440e88adf9f1c54b7#body_text
is schema:about of	named entity 'gramicidin' named entity 'Vpu' named entity 'peptide' named entity 'binding site' named entity 'Vpu' named entity 'anions and cations' named entity 'N,N-dimethylformamide' named entity 'peptide' named entity 'channel conductance' named entity 'tryptophan' named entity 'NaBr' named entity 'integral membrane protein' named entity 'Vpu' named entity 'peptide' named entity 'tryptophan' named entity 'HATU' named entity 'ion' named entity 'photosynthetic reaction centre' named entity 'reverse-phase HPLC' named entity 'anions' named entity 'serine' named entity 'ion' named entity 'Vpu' named entity 'ion channel' named entity 'NaCl' named entity 'amino acids' named entity 'cytoplasmic' named entity 'leucine' named entity 'binding site' named entity 'tryptophan' named entity 'coronavirus' named entity 'Human Immunodeficiency virus' named entity 'oleoyl' named entity 'hexafluorophosphate' named entity 'Vpu' named entity 'histogram' named entity 'hydrophobic' named entity 'molecular level' named entity 'phosphocholine' named entity 'Manchester' named entity 'Vpu' named entity 'cations and anions' named entity 'peptides' named entity 'substrates' named entity 'Vpu' named entity 'HIV-1' named entity 'ion' named entity 'ionophores' named entity 'electron density' named entity 'KCl' named entity 'liquid crystal' named entity 'peptides' named entity 'salt' named entity 'serine' named entity 'dualism' named entity 'HIV-1' named entity 'tetramethyl' named entity 'anions' named entity 'Vpu' named entity 'arginine' named entity 'salt' named entity 'Vpu' named entity 'salting-out' named entity 'peptide' named entity 'lipids' named entity 'chloroform' named entity 'KCl' named entity 'ion' named entity 'tryptophan' named entity '250 mm' named entity 'tryptophan' named entity 'Vpu' named entity 'lipid' named entity 'vesicles' named entity 'lipid bilayers'

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