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  • 1
    Electronic Resource
    Electronic Resource
    Staphylococcal nuclease reviewed: A Prototypic study in contemporary enzymology. II. Solution studies of the nucleotide binding site and the effects of nucleotide binding. (1979)
    Springer
    Molecular and cellular biochemistry 23 (1979), S. 3-16 
    Details
    ISSN: 1573-4919
    Keywords: Nuclease ; Staphylococcal Nuclease ; Micrococcal Nuclease ; Enzyme Function and Structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This is the second of a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses studies in solution delineating the extent of the binding site of the enzyme and identifying some of the particular amino acid residues that form this site. In addition, the effects of the very potent inhibitory combination of thymidine-3′,5′-diphosphate and Ca2+ on the conformation of the enzyme and its physical, chemical and enzymological properties will be reviewed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00226675
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology (1979)
    Springer
    Molecular and cellular biochemistry 23 (1979), S. 131-141 
    Details
    ISSN: 1573-4919
    Keywords: Nuclease ; Staphylococcal Nuclease ; Micrococcal Nuclease ; Protein Folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This is the last in a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3′-nucleotidohydrolase, EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses the use of the nuclease as a model system for the study of the mechanisms and energetics of the folding-unfolding reaction in proteins and for the study of the interrelationships between amino acid sequence and three-dimensional structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219452
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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