ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 2-phenylglycerol  (1)
  • brain  (1)
  • histones  (1)
  • 1
    Electronic Resource
    Electronic Resource
    2-Phenylglycerol: crystal structure and conformational considerations pertaining to formation of its related oxetane (2000)
    Springer
    Journal of chemical crystallography 30 (2000), S. 83-90 
    Details
    ISSN: 1572-8854
    Keywords: 2-phenylglycerol ; x-ray structure ; computational studies ; conformations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract 2-Phenylglycerol has been crystallized, structurally characterized, and its related conformations considered by ab initio calculations at the HF/6-31G* level. C9H12O3. $$ \frac{1}{2} $$ H2O, P21,a = 5.8786(1), b = 28.6605(7), c = 10.5553(3) Å, β = 90.187 (1)° at 100(1) K, Z = 8, R = 0.0424 for 5913 unique observed reflections. The asymmetric unit contains four molecules of the title compound and two molecules of water. The structures are characterized by extensive intermolecular hydrogen bonds. The packing is dominated by a hydrophilic hydrogen bonded layer with the hydrophobic phenyl rings forming a herringbone packed intermediate layer. Computational studies suggest that an increase in energy of about 13 kcal/mol can provide for significant conformational flexibility, including the traversal of an orientation that is appropriately aligned with the reaction trajectory needed for closure to the oxetane. Progression along this reaction coordinate, however, will probably require at least another 15 kcal/mol in the gas phase in order to bring the two SN2 species into a proximity which approaches that of the oxetane's C-O bond distance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009558410259
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Regulation of fungal proteolysis on cyclic AMP-dependent protein kinase, cyclic AMP phosphodiesterase, glycogen synthase and histones (1991)
    Springer
    Molecular and cellular biochemistry 102 (1991), S. 173-181 
    Details
    ISSN: 1573-4919
    Keywords: protease ; protein kinase ; phosphodiesterase ; glycogen synthase ; histones
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Limited proteolysis of catalytic and regulatory subunits of cyclic AMP-dependent protein kinase (A-pk), cyclic AMP phosphodiesterase, glycogen synthase, and histones by fungal protease (type XIX) was analyzed by the digested peptide bands in SDS polyacrylamide gel electrophoresis. The modulatory effects on proteolysis by nucleotides, polypeptides, and phospholipids may greatly depend on the intrinsic nature of substrates. The proteolysis of the regulatory subunit of A-pk and glycogen synthase was not regulated by nucleotides and nucleic acids. In comparison, phosphatidyl serine, cardiolipin, and pepstatin A stimulated the proteolysis of the catalytic subunit of A-pk. Whereas, λDNA (Hind III digest), t-RNA, GTP, phosphatidyl serine, sphingosine inhibited the proteolysis of cyclic AMP phosphodiesterase. Moreover, MS2 RNA, λDNA, t-RNA, dGTP, Phosphatidyl serine, phosphatidyl inositol, antipain, and chymostatin exerted inhibitory proteolytic effect on histone VIII-S. Some of these agents also had similar inhibitory effect on other types of histones (types III-S and VII-S). The inhibitory effect of phosphatidyl serine on proteolysis of histone may be due to their interaction which was monitored by the drastic increase of uv absorbance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00234575
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Regulatory effects of S-100 protein and parvalbumin on protein kinases and phosphoprotein phosphatases from brain and skeletal muscle (1986)
    Springer
    Molecular and cellular biochemistry 71 (1986), S. 19-24 
    Details
    ISSN: 1573-4919
    Keywords: S-100 protein ; parvalbumin ; protein kinase ; phosphoprotein phosphatase ; brain ; skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary In the eluted fractions of histone-treated crude extracts separated by Sephadex G-200 filtration, multiple protein kinase (PK) activities, including three from brain and two from skeletal muscle, were augmented by both S-100 protein and parvalbumin on the phosphorylation of endogenous substrates. One additional PK activity suppressed by both S-100 and parvalbumin was also found in muscle. In comparison, phosphoprotein phosphatases (PPase), which were also prepared by the same procedure of initial step of histone-treatment followed by the steps of Bio-Gel P-6DG for brain and DNA-cellulose for muscle, were all activated by S-100 while inhibited by parvalbumin and phosphatidylserine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219324
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...