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  • 1
    Electronic Resource
    Electronic Resource
    Prediction of the structure of GroES and its interaction with GroEL (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 22 (1995), S. 199-209 
    Details
    ISSN: 0887-3585
    Keywords: chaperonins ; electron microscopy ; FTIR ; molecular modeling ; structure prediction ; contact prediction ; active site prediction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The three-dimensional structure of the GroES monomer and its interaction with GroEL has been predicted using a combination of prediction tools and experimental data obtained by biophysical [electron microscope (EM), Fourier transform infrared (FTIR), and nuclear magnetic resonance (NMR)] and biochemical techniques. The GroES monomer, according to the prediction, is composed of eight β-strands forming a β-barrel with loose ends. In the model, β-strands 5-8 run along the outer surface of GroES, forming an antiparallel β-sheet with β4 loosely bound to one of the edges. β-strands 1-3 would then be parallel and placed in the interior of the molecule. Loops 1-3 would face the internal cavity of the GroEL-GroES complex, and together with conserved residues in loops 5 and 7, would form the active surface interacting with GroEL. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340220302
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  • 2
    Electronic Resource
    Electronic Resource
    Membrane destabilization induced by the human immunodeficiency virus type-1 fusion peptide (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 365-369 
    Details
    ISSN: 1573-3904
    Keywords: Conformational switching ; Membrane fusion ; Peptide conformation ; Peptide-lipid interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The human immunodeficiency virus type-1 (HIV-1) fusionpeptide, corresponding to a sequence of 23 amino acidresidues at the N-terminus of the spike transmembranesubunit gp41, has the capacity to destabilizenegatively charged and neutral large unilamellarvesicles, representing, respectively, the acidic andthe neutral fraction of the plasma membrane lipids ofviral target cells. As revealed by infraredspectroscopy, the peptide associated with the vesiclesmay exist in different conformations. In negativelycharged membranes the structure is mainly anα-helix, while in Ca2+-neutralizednegatively charged membranes the conformation switchesto a predominantly extended conformation. In membranescomposed of zwitterionic phospholipids andcholesterol, the peptide also adopts a predominantextended structure. The α-helical structurepermeabilizes negatively charged vesicles but does notinduce membrane fusion. The peptide in β-typeconformation, on the other hand, permeabilizes neutralmembranes and triggers fusion. As seen by31P NMR, the latter structure also exhibits thecapacity to alter the lamellar organization of the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008869409753
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Membrane destabilization induced by the human immunodeficiency virus type-1 fusion peptide (1997)
    Springer
    International journal of peptide research and therapeutics 4 (1997), S. 365-369 
    Details
    ISSN: 1573-3904
    Keywords: Conformational switching ; Membrane fusion ; Peptide conformation ; Peptide-lipid interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The human immunodeficiency virus type-1 (HIV-1) fusion peptide, corresponding to a sequence of 23 amino acid residues at the N-terminus of the spike transmembrane subunit gp41, has the capacity to destabilize negatively charged and neutral large unilamellar vesicles, representing, respectively, the acidic and the neutral fraction of the plasma membrane lipids of viral target cells. As revealed by infrared spectroscopy, the peptide associated with the vesicles may exist in different conformations. In negatively charged membranes the structure is mainly an α-helix, while in Ca2+-neutralized negatively charged membranes the conformation switches to a predominantly extended conformation. In membranes composed of zwitterionic phospholipids and cholesterol, the peptide also adopts a predominant extended structure. The α-helical structure permeabilizes negatively charged vesicles but does not induce membrane fusion. The peptide in β-type conformation, on the other hand, permeabilizes neutral membranes and triggers fusion. As seen by31P NMR, the latter structure also exhibits the capacity to alter the lamellar organization of the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02442901
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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