Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    The Erythrocyte/Brain Glucose Transporter (GLUT1) May Adopt a Two–Channel Transmembrane α/β Structure. (1996)
    Springer
    Journal of molecular modeling 2 (1996), S. 27-45 
    Details
    ISSN: 0948-5023
    Keywords: GLUT1 ; Glucose transport ; Structure ; Transmembrane protein ; α/β structure ; Modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract There are two models of topology for the membrane domains of the erythrocyte/brain facilitative glucose transporter, GLUT1. The first is composed of 12 membrane–spanning α–helices, the second of 16 membrane-spanning β-strands. We have used Jähnig′s and Eisenberg′s methods to identify possible transmembrane segments (10 spanning α-helices and 4 β-strands). The topology proposed is more consistent with available experimental data from FTIR, CD and mapping experiment than the previous models . We suggest that GLUT1 might form two channels, one of which is responsible for glucose transport. This agrees with the theoretical and experimental arguments. Finally, an analysis of the mutation periodicity and of the mean hydrophobicity for the GLUT family is provided in order to evaluate the packing of the protein in the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s008940050018
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Are Amphipathic Asymmetric Peptides Ubiquitous Structures for Membrane Destabilisation? (1997)
    Springer
    Journal of molecular modeling 3 (1997), S. 203-215 
    Details
    ISSN: 0948-5023
    Keywords: Keywords: Tilted peptides ; membrane destabilisation ; signal sequences ; lipases ; membrane proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The fusion of some viruses (SIV, BLV, etc) to host cells implicates short fragments of the fusion protein that are asymmetric amphipathic helices in molecular modelling. The tilted orientation of these fragments at a water/lipid interface is directly related to their fusogenic capacity. On this basis, we have searched for fragments of sequences corresponding to "viral fusion peptides" in other proteins. We have developed a strategy to detect them from primary sequences. Many candidates were detected, especially in transmembrane areas of membranous proteins, in signal sequences and in globular proteins. We suggest that they are involved in the dynamics of lipid-protein interactions
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s008940050032
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...