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  • 11
    Electronic Resource
    Electronic Resource
    β-Lactamases as models for protein-folding studies (1998)
    Springer
    Cellular and molecular life sciences 54 (1998), S. 372-377 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Protein folding; β-lactamase; cis-trans isomerization; folding intermediates; molten globule.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. This review traces some of the key features of the folding of β-lactamases and their relevance to the way proteins fold in general. Studies on the enzymes have highlighted the nature and role of equilibrium and transient condensed states. The kinetics of folding are multiphasic, and when monitored by acrylamide quenching of the tryptophan fluorescence, an early phase provides evidence for the transient accumulation of a nonnative intermediate involving burial of tryptophan in a nonpolar environment. Intermediate phases can be understood in terms of progressive folding of different parts of the molecule. The later, slow phases are associated with proline isomerization in the TEM-1 enzyme and, in its P167T mutant form, with isomerization from trans to cis of the E166 T167 peptide bond. Coupled with kinetic and X-ray crystallographic studies of the β-lactamase from Staphylococcus aureus and its D179Q mutant, it appears that the final stage of folding is that of collapse and packing of the Ω-loop on to the main body of the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050166
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  • 12
    Electronic Resource
    Electronic Resource
    Molten globule intermediates and protein folding (1991)
    Springer
    European biophysics journal 19 (1991), S. 221-229 
    Details
    ISSN: 1432-1017
    Keywords: Protein folding ; Folding intermediate ; Molten globule ; Compact states
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The background to the concept of the term “molten globule” as a description of intermediates observed in the folding of globular proteins is discussed. These compact intermediates are characterised by certain properties including the presence of secondary structure and considerable conformational mobility compared to the native, functional state. Those intermediates that are thermodynamically stable under mild denaturing conditions have many features in common with the transient intermediates that accumulate significantly during the process of folding. Attention is drawn to cases where the two types are however distinguished on grounds of their Stokes radius, in which cases there is currently no direct evidence for the involvement of the stable intermediates on the folding pathway. Experimental evidence relating to the early stages in folding is reviewed and compared, highlighting the temporal relationship between general collapse of the polypeptide chain and the formation of secondary structure. The continued use of the term “molten globule” is recommended where the minimum essential structural criteria for this state are met.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00183530
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  • 13
    Electronic Resource
    Electronic Resource
    A precise determination of the electroweak mixing angle from semileptonic neutrino scattering (1987)
    Springer
    The European physical journal 36 (1987), S. 611-628 
    Details
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The cross-section ratio of neutral-current and charged-current semileptonic interactions of muon-neutrinos on isoscalar nuclei has been measured with the result:R v =0.3093±0.0031 for hadronic energy larger than 4 GeV. From this ratio we determined the electroweak mixing angle sin2 θ W , wherem c is the charm-quark mass in GeV/c2. Comparison with direct measurements ofm w andm z determines the radiative shift of the intermediate boson mass Δr=0.077±0.025(exp.)±0.038(syst.), in agreement with the prediction. Assuming the validity of the electroweak standard theory we determined ϱ=0.990−0.013(m c −1.5)±0.009(exp.)±0.003(theor.).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01630598
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  • 14
    Electronic Resource
    Electronic Resource
    Book reviews (1992)
    Springer
    World journal of microbiology and biotechnology 8 (1992), S. 216-217 
    Details
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01195854
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  • 15
    Electronic Resource
    Electronic Resource
    Total cross sections of charged-current neutrino and antineutrino interactions on isoscalar nuclei (1988)
    Springer
    The European physical journal 38 (1988), S. 403-410 
    Details
    ISSN: 1434-6052
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract New measurements of the total crosssections of charged-current interactions of muonneutrinos and antineutrinos on isoscalar nuclei have been performed. Data were recorded in an exposure of the CHARM detector in an 160 GeV narrow-band beam. The antineutrino flux was determined from the measurements of the pion and kaon flux, and independently from the muon flux measured in the shield; the two methods are found to agree. The neutrino flux was determined from the muon flux ratio forv μ and $$\bar v_\mu $$ runs which was normalized to the antineutrino flux. The cross-section slopes thus determined are $$\begin{gathered} \sigma _T^{\bar v} /E = (0.335 \pm 0.004(stat) \hfill \\ \pm 0.010(syst)).10^{ - 38} cm^2 /(GeV \cdot nucleon) \hfill \\ \sigma _T^v /E = (0.686 \pm 0.002(stat) \hfill \\ \pm 0.020(syst)).10^{ - 38} cm^2 /(GeV \cdot nucleon) \hfill \\ \end{gathered} $$ The momentum sum of the quarks in the nucleon and the ratio of sea quark to total quark momentum are derived from the measurements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01584388
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