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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of the Code Relating Sequence to Secondary Structure in Proteins (1970)
    [s.l.] : Nature Publishing Group
    Nature 227 (1970), S. 62-63 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We have developed computer-aided techniques for compiling sequence and conformation data from proteins and retrieving it in a form pertinent to the code relating sequence to conformation. We treat the chain of amino-acids as a message and apply information theory techniques. There are many ways of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/227062a0
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  • 2
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    Elderly Women and Fear of Violent Crime: The Least Likely Victims? A Reconsideration of the Extent and Nature of Risk (1995)
    London : Periodicals Archive Online (PAO)
    British Journal of Criminology, Delinquency and Deviant Social Behaviour. 35 (1995) 584 
    Details
    ISSN: 0007-0955
    Topics: Law
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:4065-1995-035-00-000017
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  • 3
    Electronic Resource
    Electronic Resource
    Art of the insoluble (1980)
    [s.l.] : Nature Publishing Group
    Nature 286 (1980), S. 830-830 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] MEDAWAR has reminded us that the pursuit of science is the art of the soluble. This book is about the art of the insoluble. To judge by the number of monographs recently published on the subject, interest in the hydrophobic effect and its involvement in the stabilization of biological structures ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/286830a0
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  • 4
    Electronic Resource
    Electronic Resource
    Sub-unit Nature of Catalase Compound II (1968)
    [s.l.] : Nature Publishing Group
    Nature 217 (1968), S. 1050-1050 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The catalase used in our experiments was prepared from M. lysodeikticus and had an activity2 of 6*5 x 107 M-1 s-1 and an RZ value of 0-8; sedimentation velocity experiments showred no lower molecular weight impurities. Catalase was partially converted to compound II by the addition to catalase ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2171050a0
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  • 5
    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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  • 6
    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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  • 7
    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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