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
  • 1
    facet.materialart.
    Unknown
    Structural and mechanistic basis of anti-termination of Rho-dependent transcription termination by bacteriophage P4 capsid protein Psu (2013)
    Oxford University Press
    Details
    Publication Date: 2013-08-09
    Description: The conserved bacterial transcription terminator, Rho, is a potent target for bactericidal agents. Psu, a bacteriophage P4 capsid protein, is capable of inducing anti-termination to the Rho-dependent transcription termination. Knowledge of structural and mechanistic basis of this anti-termination is required to design peptide-inhibitor(s) of Rho from Psu. Using suppressor genetics, cross-linking, protein foot-printing and FRET analyses, we describe a conserved disordered structure, encompassing 139–153 amino acids of Rho, as the primary docking site for Psu. Also a neighbouring helical structure, comprising 347–354 amino acids, lining its central channel, plays a supportive role in the Rho–Psu complex formation. Based on the crystal structure of Psu, its conformation in the capsid of the P4 phage, and its interacting regions on Rho, we build an energy-minimized structural model of the Rho:Psu complex. In this model, a V-shaped dimer of Psu interacts with the two diagonally opposite subunits of a hexameric Rho, enabling Psu to form a ‘lid’ on the central channel of the latter. We show that this configuration of Psu makes the central channel of Rho inaccessible, and it causes a mechanical impediment to its translocase activity.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-10-14
    Description: The APOBEC family members are involved in diverse biological functions. APOBEC3G restricts the replication of human immunodeficiency virus (HIV), hepatitis B virus and retroelements by cytidine deamination on single-stranded DNA or by RNA binding. Here we report the high-resolution crystal structure of the carboxy-terminal deaminase domain of APOBEC3G (APOBEC3G-CD2) purified from Escherichia coli. The APOBEC3G-CD2 structure has a five-stranded beta-sheet core that is common to all known deaminase structures and closely resembles the structure of another APOBEC protein, APOBEC2 (ref. 5). A comparison of APOBEC3G-CD2 with other deaminase structures shows a structural conservation of the active-site loops that are directly involved in substrate binding. In the X-ray structure, these APOBEC3G active-site loops form a continuous 'substrate groove' around the active centre. The orientation of this putative substrate groove differs markedly (by 90 degrees) from the groove predicted by the NMR structure. We have introduced mutations around the groove, and have identified residues involved in substrate specificity, single-stranded DNA binding and deaminase activity. These results provide a basis for understanding the underlying mechanisms of substrate specificity for the APOBEC family.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2714533/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2714533/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Lauren G -- Prochnow, Courtney -- Chang, Y Paul -- Bransteitter, Ronda -- Chelico, Linda -- Sen, Udayaditya -- Stevens, Raymond C -- Goodman, Myron F -- Chen, Xiaojiang S -- R01 AI055926/AI/NIAID NIH HHS/ -- R01 AI055926-05/AI/NIAID NIH HHS/ -- England -- Nature. 2008 Nov 6;456(7218):121-4. doi: 10.1038/nature07357. Epub 2008 Oct 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18849968" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents ; *Catalytic Domain ; Crystallography, X-Ray ; Cytidine Deaminase/*chemistry/genetics/isolation & purification/*metabolism ; DNA, Single-Stranded/metabolism ; Escherichia coli ; Humans ; Models, Molecular ; Muscle Proteins/chemistry ; Mutant Proteins/chemistry/genetics/metabolism ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Protein Structure, Secondary ; Structural Homology, Protein ; Structure-Activity Relationship ; Substrate Specificity
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    Electronic Resource
    Electronic Resource
    Soil organic carbon stocks, storage profile and microbial biomass under different crop management systems in a tropical agricultural ecosystem (2000)
    Springer
    Biology and fertility of soils 32 (2000), S. 273-278 
    Details
    ISSN: 1432-0789
    Keywords: Key words Carbon stocks ; Microbial biomass ; Tropical agriculture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract  We investigated the soil organic C and N stocks, storage profiles and microbial biomass as influenced by different crop management systems in a tropical agricultural ecosystem. The different crop management systems significantly affected the C and N stocks and microbial biomass C and N at different soil depths. Amongst the systems evaluated, the rice-wheat system maintained a higher soil organic C content. Inclusion of legumes in the system improved the soil organic matter level and also soil microbial biomass activity, vital for the nutrient turnover and long-term productivity of the soil. Irrespective of the cropping system, approximately 58.4%, 25.7% and 15.9% of the C was distributed in 0–15, 15–30 and 30–60 cm depths, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003740000248
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Structural Characterization of Titanium Nitride Coatings on AISI M2 Steel (2007)
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 554 (Aug. 2007), p. 219-224 
    Details
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: In this work, some surface properties of AISI M2 steel were improved by a thermoreactivedeposition process. Gas nitriding was realized on AISI M2 steel at 550°C for 2 h in anammoniac atmosphere and then, titanizing treatment performed on pre-nitrided steel in the powdermixture consisting of ferro-titanium, ammonium chloride and alumina at 1000°C for 1-4 h.Structural characterization of titanium nitride layer formed on the surface of AISI M2 steel wascarried out by using optical microscopy, scanning electron microscopy, electron microprobe and Xraydiffraction (XRD) analysis. The hardness measurements of titanium nitride layer wereconducted under 10 g loads by using Vickers microhardness indenter. Structural analysis studiesshowed that titanium nitride layers formed on the AISI M2 steel samples were smooth, compact andhomogeneous. XRD analysis show that the coating layer formed on the steel samples includes TiN,Fe6Mo7N2, C0.7N0.3Ti, C0.3N0.7Ti and V2N phases. The hardness of titanium nitride layers formed onthe steel samples is between 2040±186 and 2418±291 HV0.01. The thickness of titanium nitridelayer formed on the steel samples ranged from 3.86±0.43 9m to 6.13±0.47 9m, depending ontreatment time
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/16/transtech_doi~10.4028%252Fwww.scientific.net%252FMSF.554.219.pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of Niobium Carbonitride Coating on AISI D2 Steel (2007)
    s.l. ; Stafa-Zurich, Switzerland
    Materials science forum Vol. 554 (Aug. 2007), p. 213-217 
    Details
    ISSN: 1662-9752
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Thermo-diffusion coatings containing Nitrogen, Carbon and Niobium (N+C+Nb) onAISI D2 steel have been carried out by an initial tufftriding process followed by saturation withNiobium. The properties of the diffusion layer, namely microstructure, phase composition andmicro-hardness of the Niobium carbonitride layer, have been studied. The influence of treatmenttime of Niobizing on the thickness of the metallized layer and its phase composition has beenstudied. Nitriding treatment was performed at 575°C for 2 h. Then, the Niobizing treatment wasperformed by pack method in the powder mixture consisting of ferro-Niobium, ammonium chlorideand alumina at 1000°C for 1–4 h. The phases formed on the Niobium carbonitride coated steel wereNbN and NbC, confirmed by X-ray diffraction (XRD) analysis. The longer the treatment times, thethicker the Niobium carbonitride layer became. The thickness of Niobium carbonitride layer waschanging between 6.53 3m and 17.45 3m, depending on treatment time and temperature. Themicrohardness of Niobium carbonitride layer formed on the AISI D2 steel was changing between2132±203 and 2814±245 HV0.01 from surface to interior
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/02/16/transtech_doi~10.4028%252Fwww.scientific.net%252FMSF.554.213.pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Structure of a Kunitz-Type Chymotrypsin from Winged Bean Seeds at 2.95 Å Resolution (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 521-528 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Thc crystal structure of an α-chymotrypsin inhibitor (P6122; a = 61.4, c = 210.9 Å) isolated from winged bean (Psophocarpus. tetragonolobus) seeds has been determined at 2.95 Å resolution by the molecular-replacement method using the 2.6 Å coordinates of Erythrina trypsin inhibitor (ETI) as the starting model (57% sequence homology). This protease inhibitor, WCI, belongs to the Kunitz (STI) family and is a single polypeptide chain with 183 amino-acid residues having a molecular weight of 20 244 Da. Structure refinement with RESTRAIN and X-PLOR has led to a crystallographic R factor of 19.1% for 3469 observed reflections (I 〉 2σ) in the resolution range 8–2.95 Å. A total of 56 water molecules have been incorporated in the refined model containing 181 amino-acid residues. In the refined structure the deviations of bond lengths and bond angles from ideal values are 0.015 Å and 2.2°, respectively. The inhibitor molecule is spherical and consists of 12 antiparallel β-strands with connecting loops arranged in a characteristic folding (a six-stranded β-barrel and a six-stranded lid on one hollow end of the barrel) common to other homologous serine protease inhibitors in the Kunitz (STI) family as well as to some non-homologous proteins like interleukin-lα and interleukin-lβ. In the structure the conformation of the protruding reactive-site loop is stabilized through hydrogen bonds mainly formed by the side chain of Asnl4, which intrudes inside the cavity of the reactive-site loop, with the side-chain and main-chain atoms of some residues in the loop region. A pseudo threefold axis exists parallel to the barrel axis of the structure. Each of the three subdomains comprises of four β-strands with connecting loops.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996000224
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 Å resolution (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1814-1821 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of a Kunitz-type double-headed α-chymotrypsin inhibitor from winged bean seeds has been refined at 2.13 Å resolution using data collected from cryo-cooled (90 K) crystals which belong to the hexagonal space group P6122 with unit-cell parameters a = b = 60.84, c = 207.91 Å. The volume of the unit cell is reduced by 5.3% on cooling. The refinement converged to an R value of 20.0% (Rfree = 25.8%) for 11100 unique reflections and the model shows good stereochemistry, with r.m.s. deviations from ideal values for bond lengths and bond angles of 0.011 Å and 1.4°, respectively. The structural architecture of the protein consists of 12 antiparallel β-strands joined in the form of a characteristic β-trefoil fold, with the two reactive-site regions, Asn38–Leu43 and Gln63–Phe68, situated on two external loops. Although the overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the side chains of a few surface residues. A total of 176 ordered water molecules and five sulfate ions are included in the model.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999009877
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Improving the Surface Properties of Ductile Irons by Boronizing (2004)
    s.l. ; Stafa-Zurich, Switzerland
    Key engineering materials Vol. 264-268 (May 2004), p. 541-544 
    Details
    ISSN: 1013-9826
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/01/48/transtech_doi~10.4028%252Fwww.scientific.net%252FKEM.264-268.541.pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Kinetics of Boride Layers Formed on the Surface of AISI 4140 Steel (2004)
    s.l. ; Stafa-Zurich, Switzerland
    Key engineering materials Vol. 264-268 (May 2004), p. 565-568 
    Details
    ISSN: 1013-9826
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/01/48/transtech_doi~10.4028%252Fwww.scientific.net%252FKEM.264-268.565.pdf
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Thermo-Reactive Diffusion Vanadium Nitride Coatings on AISI 1020 Steel (2004)
    s.l. ; Stafa-Zurich, Switzerland
    Key engineering materials Vol. 264-268 (May 2004), p. 577-580 
    Details
    ISSN: 1013-9826
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/01/48/transtech_doi~10.4028%252Fwww.scientific.net%252FKEM.264-268.577.pdf
    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...