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  • 1
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    Extensible collagen in mussel byssus: a natural block copolymer (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-20
    Description: To adhere to solid surfaces, marine mussels produce byssal threads, each of which is a stiff tether at one end and a shock absorber with 160 percent extensibility at the other end. The elastic extensibility of proximal byssus is extraordinary given its construction of collagen and the limited extension (less than 10 percent) of most collagenous materials. From the complementary DNA, we deduced that the primary structure of a collagenous protein (preCol-P) predominating in the extensible proximal portion of the threads encodes an unprecedented natural block copolymer with three major domain types: a central collagen domain, flanking elastic domains, and histidine-rich terminal domains. The elastic domains have sequence motifs that strongly resemble those of elastin and the amorphous glycine-rich regions of spider silk fibroins. Byssal thread extensibility may be imparted by the elastic domains of preCol-P.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coyne, K J -- Qin, X X -- Waite, J H -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1830-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉College of Marine Studies and Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295275" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/chemistry ; Amino Acid Sequence ; Animals ; Base Sequence ; Biopolymers/chemistry ; Bivalvia/*chemistry/genetics ; Collagen/*chemistry/genetics ; DNA, Complementary ; Elasticity ; Elastin/chemistry/genetics ; Fibroins/chemistry ; Glycine/chemistry ; Histidine/chemistry ; Molecular Sequence Data ; Proline/chemistry ; Protein Conformation ; Protein Precursors/*chemistry/genetics ; Protein Structure, Secondary ; Sequence Alignment ; Serine/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A potential mediator of collagenous block copolymer gradients in mussel byssal threads (1998)
    National Academy of Sciences
    Details
    Publication Date: 1998-09-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 3
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    Structural insights into Paf1 complex assembly and histone binding (2013)
    Oxford University Press
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    Publication Date: 2013-12-07
    Description: The highly conserved Paf1 complex (PAF1C) plays critical roles in RNA polymerase II transcription elongation and in the regulation of histone modifications. It has also been implicated in other diverse cellular activities, including posttranscriptional events, embryonic development and cell survival and maintenance of embryonic stem cell identity. Here, we report the structure of the human Paf1/Leo1 subcomplex within PAF1C. The overall structure reveals that the Paf1 and Leo1 subunits form a tightly associated heterodimer through antiparallel beta-sheet interactions. Detailed biochemical experiments indicate that Leo1 binds to PAF1C through Paf1 and that the Ctr9 subunit is the key scaffold protein in assembling PAF1C. Furthermore, we show that the Paf1/Leo1 heterodimer is necessary for its binding to histone H3, the histone octamer, and nucleosome in vitro . Our results shed light on the PAF1C assembly process and substrate recognition during various PAF1C-coordinated histone modifications.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 4
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    Structural basis for blue-green light harvesting and energy dissipation in diatoms (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉Diatoms are abundant photosynthetic organisms in aquatic environments and contribute 40% of its primary productivity. An important factor that contributes to the success of diatoms is their fucoxanthin chlorophyll a/c-binding proteins (FCPs), which have exceptional light-harvesting and photoprotection capabilities. Here, we report the crystal structure of an FCP from the marine diatom 〈i〉Phaeodactylum tricornutum〈/i〉, which reveals the binding of seven chlorophylls (Chls) a, two Chls c, seven fucoxanthins (Fxs), and probably one diadinoxanthin within the protein scaffold. Efficient energy transfer pathways can be found between Chl a and c, and each Fx is surrounded by Chls, enabling the energy transfer and quenching via Fx highly efficient. The structure provides a basis for elucidating the mechanisms of blue-green light harvesting, energy transfer, and dissipation in diatoms.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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