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  • Atomic and molecular processes in external fields, including interactions with strong fields and short pulses  (2)
  • Aminoacylase  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Inactivation and unfolding of aminoacylase during denaturation in sodium dodecyl sulfate solutions (1995)
    Springer
    The protein journal 14 (1995), S. 349-357 
    Details
    ISSN: 1573-4943
    Keywords: Aminoacylase ; sodium dodecyl sulfate ; inactivation ; conformational change
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract During denaturation by sodium dodecyl sulfate (SDS), aminoacylase shows a rapid decrease in activity with increasing concentration of the detergent to reach complete inactivation at 1.0 mM SDS. The denatured minus native-enzyme difference spectrum showed two negative peaks at 287 and 295 nm. With the increase of concentration of SDS, both negative peaks increased in magnitude to reach maximal values at 5.0 mM SDS. The fluorescence emission intensity of the enzyme decreased, whereas there was no red shift of emission maximum in SDS solutions of increasing concentration. In the SDS concentration regions employed in the present study, no marked changes of secondary structure of the enzyme have been observed by following the changes in far-ultraviolet CD spectra. The inactivation of this enzyme has been followed and compared with the unfolding observed during denaturation in SDS solutions. A marked inactivation is already evident at low SDS concentration before significant conformational changes can be detected by ultraviolet absorbance and fluorescence changes. The inactivation rate constants of free enzyme and substrate-enzyme complex were determined by the kinetics method of the substrate reaction in the presence of inactivator previously described by Tsou [Tsou (1988),Adv. Enzymol. Related Areas Mol. Biol. 61, 381–436]. It was found that substrate protects against inactivation and at the same SDS concentrations, the inactivation rate of the free enzyme is much higher than the unfolding rate. The above results show that the active sites of metal enzyme containing Zn2+ are also situated in a limited and flexible region of the enzyme molecule that is more fragile to denaturants than the protein as a whole.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886792
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    Paper (German National Licenses)
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  • 2
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    Photodissociation of Br_{2} molecules in an intense femtosecond laser field (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-11-25
    Description: Author(s): Jian Zhang, Shian Zhang, Yan Yang, Shengzhi Sun, Hua Wu, Jing Li, Yuting Chen, Tianqing Jia, Zugeng Wang, Fanao Kong, and Zhenrong Sun We experimentally demonstrate the photodissociation process of Br 2 molecules in the intense femtosecond laser field by a dc-sliced ion velocity map imaging technique. We show that four fragment ions Br n+   ( n=1–4 ) are observed, and their kinetic energy increases while their angular distribution decrea... [Phys. Rev. A 90, 053428] Published Mon Nov 24, 2014
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Channel-resolved multiorbital double ionization of molecular ${\mathrm{Cl}}_{2}$ in an intense femtosecond laser field (2018)
    American Physical Society (APS)
    Details
    Publication Date: 2018-10-02
    Description: Author(s): Jian Zhang, Yan Yang, Zhipeng Li, Haitao Sun, Shian Zhang, and Zhenrong Sun We measure the sequential double ionization and the subsequent Coulomb explosion of molecular Cl 2 in an intense femtosecond laser field by using the dc-sliced ion imaging technique. The results indicate that not only the highest occupied molecular orbital (HOMO) but also the next two lower-lying mol... [Phys. Rev. A 98, 043402] Published Mon Oct 01, 2018
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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