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  • 1
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    Reshaping of the conformational search of a protein by the chaperone trigger factor (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-07-09
    Description: Protein folding is often described as a search process, in which polypeptides explore different conformations to find their native structure. Molecular chaperones are known to improve folding yields by suppressing aggregation between polypeptides before this conformational search starts, as well as by rescuing misfolds after it ends. Although chaperones have long been speculated to also affect the conformational search itself--by reshaping the underlying folding landscape along the folding trajectory--direct experimental evidence has been scarce so far. In Escherichia coli, the general chaperone trigger factor (TF) could play such a role. TF has been shown to interact with nascent chains at the ribosome, with polypeptides released from the ribosome into the cytosol, and with fully folded proteins before their assembly into larger complexes. To investigate the effect of TF from E. coli on the conformational search of polypeptides to their native state, we investigated individual maltose binding protein (MBP) molecules using optical tweezers. Here we show that TF binds folded structures smaller than one domain, which are then stable for seconds and ultimately convert to the native state. Moreover, TF stimulates native folding in constructs of repeated MBP domains. The results indicate that TF promotes correct folding by protecting partially folded states from distant interactions that produce stable misfolded states. As TF interacts with most newly synthesized proteins in E. coli, we expect these findings to be of general importance in understanding protein folding pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mashaghi, Alireza -- Kramer, Gunter -- Bechtluft, Philipp -- Zachmann-Brand, Beate -- Driessen, Arnold J M -- Bukau, Bernd -- Tans, Sander J -- England -- Nature. 2013 Aug 1;500(7460):98-101. doi: 10.1038/nature12293. Epub 2013 Jul 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉FOM institute AMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23831649" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cytosol/metabolism ; Escherichia coli/chemistry/metabolism ; Escherichia coli Proteins/*metabolism ; Maltose-Binding Proteins/biosynthesis/*chemistry/*metabolism ; Models, Molecular ; Molecular Chaperones/*metabolism ; Optical Tweezers ; Peptides/chemistry/metabolism ; Peptidylprolyl Isomerase/*metabolism ; Protein Biosynthesis ; Protein Conformation ; *Protein Folding ; Protein Refolding ; Protein Stability ; Protein Structure, Tertiary ; Ribosomes/metabolism ; Spectroscopy, Fourier Transform Infrared
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Operon structure and cotranslational subunit association direct protein assembly in bacteria (2015)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2015-09-26
    Description: Assembly of protein complexes is considered a posttranslational process involving random collision of subunits. We show that within the Escherichia coli cytosol, bacterial luciferase subunits LuxA and LuxB assemble into complexes close to the site of subunit synthesis. Assembly efficiency decreases markedly if subunits are synthesized on separate messenger RNAs from genes integrated at distant chromosomal sites. Subunit assembly initiates cotranslationally on nascent LuxB in vivo. The ribosome-associated chaperone trigger factor delays the onset of cotranslational interactions until the LuxB dimer interface is fully exposed. Protein assembly is thus directly coupled to the translation process and involves spatially confined, actively chaperoned cotranslational subunit interactions. Bacterial gene organization into operons therefore reflects a fundamental cotranslational mechanism for spatial and temporal regulation that is vital to effective assembly of protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shieh, Yu-Wei -- Minguez, Pablo -- Bork, Peer -- Auburger, Josef J -- Guilbride, D Lys -- Kramer, Gunter -- Bukau, Bernd -- New York, N.Y. -- Science. 2015 Nov 6;350(6261):678-80. doi: 10.1126/science.aac8171. Epub 2015 Sep 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. ; European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany. ; European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany. Max-Delbruck-Centre for Molecular Medicine, Robert-Rossle-Strasse 10, 13125 Berlin, Germany. ; Center for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. Malaria Research Foundation, Post Office Box 10420, Aspen, CO 81612, USA. ; Center for Molecular Biology of the University of Heidelberg (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. bukau@zmbh.uni-heidelberg.de g.kramer@zmbh.uni-heidelberg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26405228" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*genetics/*metabolism ; Bacterial Proteins/chemistry/genetics/metabolism ; Escherichia coli ; *Gene Order ; Genes, Bacterial ; Green Fluorescent Proteins/chemistry/genetics/metabolism ; Luciferases, Bacterial/chemistry/*genetics/*metabolism ; Luminescent Proteins/chemistry/genetics/metabolism ; Molecular Chaperones/metabolism ; *Operon ; Protein Biosynthesis ; Protein Structure, Secondary ; Protein Subunits/chemistry/deficiency/genetics/metabolism ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/chemistry/genetics/metabolism ; Ribosomes/metabolism ; Vibrio/enzymology
    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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  • 3
    Electronic Resource
    Electronic Resource
    Interlaboratory study for the improvement of tributyltin determination in harbour sediment (rm 424) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Applied Organometallic Chemistry 8 (1994), S. 639-644 
    Details
    ISSN: 0268-2605
    Keywords: Interlaboratory study ; harbour sediment ; analytical quality control ; reference material ; tributyltin ; dibutyltin ; monobutyltin ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Following two interlaboratory studies on tributyltin species (TBT) in water and TBT-spiked sediment, the EC Community Bureau of Reference (BCR) (Measurements and Testing Programme) organized in 1992 an interlaboratory study on TBT in a harbour sediment (RM 424) to investigate sources of error possibly occurring in the analysis of a complicated matrix and to attempt to certify this material. The sediment was collected in the Sado Estuary (P), then carefully prepared, and its homogeneity and stability were verified. The low TBT content encountered in this material, and the high level of interferences, created difficulties with the techniques using hydride generation, whereas better agreement was obtained for other derivatization techniques with GC/FPD and GC/MS. This paper presents the results of the interlaboratory study. The reference value for TBT in this material is 20±5 ng g-1 (as TBT cation) and the indicative values for dibutyltin (DBT) and monobutyltin (MBT) are 53±19 ng g-1 (as DBT cation) and 257±54 ng g-1 (as MBT cation), respectively. Owing to the difficulties encountered, the reference material was not certified and is considered as a research material to be used for the evaluation of the performance of analytical techniques for the determination of low TBT levels in a difficult matrix.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aoc.590080714
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  • 4
    Electronic Resource
    Electronic Resource
    Certified reference material (CRM 462) for the quality control of dibutyl- and tributyl-tin determinations in coastal sediment (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Applied Organometallic Chemistry 8 (1994), S. 629-637 
    Details
    ISSN: 0268-2605
    Keywords: Certified Reference Material ; coastal sediment ; analytical quality control ; tributyltin ; dibutyltin ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Determinations of tributyltin (TBT) species, along with the degradation products mono- and dibutyltin (MBT and DBT), are routinely carried out by a number of laboratories to ascertain the level of organotin contamination of the marine enviroment, particularly in water, sediment and biota. In order to improve and control the quality of such analyses the EC Community Bureau of Reference, BCR (Measurements and Testing Programme), has organized two interlaboratory studies on TBT in water and TBT in a spiked sediment which were followed by a certification campaign for butyltins in a coastal sediment (CRM 462). This material was collected in the Arcachon Bay (France), then carefully prepared (controlled oven drying) and its homogeneity and long-term stability were verified. This paper presents the certification work performed. The certified values for TBT and DBT are 70±14 ng g-1 (as TBT cation) and 128±16 ng g-1 (as DBT cation), respectively.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aoc.590080713
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