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  • 1
    Monograph available for loan
    Monograph available for loan
    The biobased economy : biofuels, materials and chemicals in the post-oil era (2010)
    London [u.a.] : Earthscan
    Details Availability
    Call number: PIK B 160-10-0025
    Description / Table of Contents: Contents: Section one - Towards sustainability: 1 General introduction ; 2 Transition towards a biobased economy ; 3 Challenges for sustainable development ; 4 Principles of plant production ; 5 Plant breeding and its role in a biobased economy ; 6 Biomass availability ; Section two - Biomass refining and conversion: Introduction to section II ; 7 Biorefineries: Giving value to sustainable biomass use ; 8 Plant production of chemical building blocks ; 9 The production of chemicals in a biobased economy ; 10 Advanced biofuels from lignocellulosic biomass ; 11Biogas ; Section three - Actor involvement: Introduction to section III ; 12 Policy making for the biobased economy ; 13 Biobased industrialization in developing countries ; 14 Biobased production chains ; 15 Biofuel policies, production, trade and land use ; 16 Public debate on sustainability of biofuels ; Section four - Transition in action: Introduction to section IV ; 17 Biodiesel from Brazil ; 18 Biobased products and bioenergy in germany ; 19 Development of the biobased economy in Canada - an overview ; 20 A biobased economy for the Netherlands ; 21 Synthesis
    Type of Medium: Monograph available for loan
    Pages: XXVI, 389 S. : graph. Darst.
    ISBN: 9781844077700
    Branch Library: PIK Library
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  • 2
    Electronic Resource
    Electronic Resource
    Secondary structure of M13 coat protein in phospholipids studied by circular dichroism, Raman, and Fourier transform infrared spectroscopy (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 12446-12454 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00097a024
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  • 3
    Electronic Resource
    Electronic Resource
    Stoichiometry, selectivity, and exchange dynamics of lipid-protein interaction with bacteriophage M13 coat protein studied by spin label electron spin resonance. Effects of protein secondary structure (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 2670-2677 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00125a006
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  • 4
    Electronic Resource
    Electronic Resource
    A small protein in model membranes: a time-resolved fluorescence and ESR study on the interaction of M13 coat protein with lipid bilayers (1992)
    Springer
    European biophysics journal 21 (1992), S. 305-311 
    Details
    ISSN: 1432-1017
    Keywords: M13 coat protein ; Lipid protein interaction ; ESR spectroscopy ; Time-resolved fluorescence spectroscopy ; Order parameter ; Diffusion coefficient
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Model membranes with unsaturated lipid chains containing various amounts of M13 coat protein in the α-helical form were studied using time-resolved fluorescence and ESR spectroscopy. The lipid-to-protein (L/P) ratios used were 〉 12 to avoid protein-protein contacts and irreversible aggregation leading to β-polymeric coat protein. In the ESR spectra of the 12-SASL probe in dioleoyl phosphatidylcholine (DOPC) bilayers no second protein induced component is observed upon incorporation of M13 coat protein. However, strong effects are detected on the ESR lineshapes upon changing the protein concentration. The ESR lineshapes are simulated by assuming a fixed ratio between the parallel (D‖) and perpendicular (D⊥) diffusion coefficients of 4, and an order parameter equal to zero. It is found that increasing the protein concentration from L/P ∞ to L/P 15 results in a decrease of the rotational diffusion coefficient D⊥ from 3.4 × 107 to 1.9 × 107 s−1. In the time-resolved fluorescence experiments with DPH-propionic acid as a probe, it is observed that increasing the M13 coat protein concentration causes an increase of the two fluorescent lifetimes, indicating an increase in bilayer order. Analysis of the time-resolved fluorescence anisotropy decay allows one to quantitatively determine the order parameters 〈P2〉 and 〈P4〉, and the rotational diffusion coefficient D⊥ of the fluorescent probe. The order parameters 〈P2〉 and 〈P4〉 increase from 0.34 to 0.55 and from 0.59 to 0.77, respectively, upon adding M13 coat protein to DOPC bilayers with an L/P ratio of 35. The rotational diffusion coefficient D⊥ of the DPH-propionic acid probe decreases on incorporating M13 coat protein, in accordance with the ESR results. It is concluded that M13 coat protein in the α-monomeric state is not able to produce a long living lipid boundary shell and consequently an immobilization of the lipids. An overall effect on the lipids is induced, resulting in a reduction in the dynamics and an increase in average lipid order. The hydrophobic region of M13 coat protein is proposed to perfectly match the lipid bilayer, resulting in a relatively small distortion of the bilayer structure of the lipid system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00188342
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  • 5
    Electronic Resource
    Electronic Resource
    The organization of genes in yeast mitochondrial DNA (1975)
    Springer
    Molecular genetics and genomics 143 (1975), S. 53-64 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. We have isolated large fragments of the mtDNA of the yeast Saccharomyces carlsbergensis and digested these with restriction endonucleases. The digestion products were separated by electrophoresis in agarose gels. 2. Endonucleases EcoRI, HindII+III, HpaI, HindIII and HapII yield 9, 11, 6, 0 and 〉80 fragments, respectively. 3. By analysis of partial digestion products and by redigesting the fragments obtained with one endonuclease with a second, we have established the order of all EcoRI and HindII+III fragments. The map is circular and its contour length is 22.1±0.35 μm, in good agreement with earlier estimates of the size of yeast mtDNA, using electron microscopy and renaturation kinetics. 4. A comparison of the fragmentation pattern of mtDNAs from S. carlsbergensis and various strains of Saccharomyces cerevisiae with endonuclease HindII+III suggests that the overall gene order is similar.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00269420
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  • 6
    Electronic Resource
    Electronic Resource
    The organization of gene in yeast mitochondrial DNA (1977)
    Springer
    Molecular genetics and genomics 157 (1977), S. 239-261 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1) We have constructed independent physical maps of the mtDNAs from three different wild-type Saccharomyces strains by double-digestion analysis and hybridization analysis, using restriction endonucleases EcoRI, HindII, HindIII, PstI, BamHI, Aval, HhaI, SalI and XhoI. Twentynine restriction enzyme sites have been localized on the mtDNA of Saccharomyces carlsbergensis, 47 on the mtDNA of Saccharomyces cerevisiae strain JS1-3D and 38 on the mtDNA of Saccharomyces cerevisiae strain KL14-4A. 2) Although the three DNAs show considerable differences in their fragmentation patterns with most nucleases tested, the overall sequence organization of the three maps of 30–40 fragments is identical. Differences in the maps can be explained by extra restriction enzyme recognition sites, possibly located on inserted pieces of DNA and by insertions and deletions. 3) Four major insertions (900, 1,500, 2,600 and 3,000 bp long) are found in KL14-4A mtDNA relative to Saccharomyces carlsbergensis mtDNA. These insertions are clustered in one quadrant of the mtDNA and account for the difference in size of these two mtDNAs (75,750 and 68,000 bp, respectively).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268660
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  • 7
    Electronic Resource
    Electronic Resource
    The construction of the physical maps of three different Saccharomyces mitochondrial DNAs (1977)
    Springer
    Molecular genetics and genomics 157 (1977), S. 271-280 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268662
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  • 8
    Electronic Resource
    Electronic Resource
    The organization of genes in yeast mitochondrial DNA (1977)
    Springer
    Molecular genetics and genomics 157 (1977), S. 263-269 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have fractionated fragments of yeast mtDNA, obtained with restriction endonucleases, on poly(U)-Sephadex columns using the procedure of Flavell and Van den Berg (FEBS Letters (1975) 58, 90–93). The poly(U) forms a triple helix with (dA·dT) clusters in duplex DNA and fractionates DNA fragments on the basis of the length and number of clusters contained in them. mtDNA fragments obtained with endonucleases PstI, BamHI, HindII, HindII+III, EcoRI, HapII and HhaI were separated by poly(U)-Sephadex in three groups: fragments not retained by the column in 2M LiCl, fragments partially retained and fragments (nearly) completely bound in 2 M LiCl and only eluted by 0.1 M LiCl. The separation obtained is adequate for analytical fractionation of fragments and it can be used for the preparative isolation of firmly-bound fragments. In mtDNA digests made with endonuclease HapII, which gives about 70 separable fragments under our conditions, only about 10% of the fragments were firmly bound to poly(U)-Sephadex. This shows that the number of (dA·dT) clusters long enough to result in binding is limited in yeast mtDNA and its suggests that large fragments are bound by only one or a few clusters. Corresponding segments of the physical map of the mtDNAs from Saccharomyces carlsbergensis and Saccharomyces cerevisiae strains JS1-3D and KL14-4A were bound to the column, showing that the (dA·dT) clusters responsible for binding are conserved in the evolution of mtDNA. However, one 3,000 bp insert, only present on KL14-4A mtDNA, causes the loss of a binding site, another long insert introduces a new binding site. Fragments firmly bound to the columns are clustered in one quadrant of the physical map of these three mtDNAs. This quadrant also contains the large insertions present in KL14-4A mtDNA and absent from S. carlsbergensis mtDNA. The possible relation between (dA·dT) clusters and insertions is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268661
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  • 9
    Electronic Resource
    Electronic Resource
    Fine structure of the 21S ribosomal RNA region on yeast mitochondrial DNA (1979)
    Springer
    Molecular genetics and genomics 168 (1979), S. 231-250 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1 We have used restriction enzyme analysis of petite mtDNAs to construct a detailed physical map of the 21S region on the mtDNA of the Saccharomyces cerevisiae strain JS1-3D. The map covers a segment of about 20,000 bp, on which the recognition sites of the enzymes HapII, HindII, HindIII, SalI, XhoI and HhaI have been localized (22 sites in total). This map has been checked in various ways against the independently constructed overall physical map of the mtDNA of strain JS1-3D. In addition, we have constructed a physical map with a resolution of about 200 bp of a HapII fragment of 1850 bp long, which carries the loci ω, RIB-1 and probably RIB-2. 2. The 21S rRNA hybridizes with the five adjacent HindII+III fragments TD9, DT19, TD15, DT14 and TT1, which lie in that order on the physical map of the 21S region. Of these, the two non-adjacent fragments TD9 and DT14 show a much stronger hybridization with 21S rRNA than DT19, TD15, and TT1. 3. The fragment DD5 (=DT19+TD15) and part of DT14 belong to a sequence of about 1000 bp, which is absent from Saccharomyces carlsbergensis mtDNA. Although DD5 and DT14 show (very weak, respectively stronger) hybridization with 21S rRNA, the 1000 bp insert probably does not code for the 21S rRNA: the 21S rRNA of S. carlsbergensis comigrates with the 21S rRNA of JS1-3D on polyacrylamide gels under denaturing conditions. 4. Fragment DT14 hybridizes with the HindII +III fragment TD9, which shows the strongest hybridization with 21S rRNA. The presence of these sequence homologies has hampered the precise mapping of the 21S rRNA cistron. Our results are compatible, however, with the hypothesis that the sequences, coding for 21S rRNA, are located on HindII+III fragments that are not adjacent on JS1-3D mtDNA, namely TD9, DT14 and TT1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271496
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  • 10
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    A small protein in model membranes: a time-resolved fluorescence and ESR study on the interaction of M13 coat protein with lipid bilayers (1992)
    Springer
    Details
    Publication Date: 1992-11-01
    Print ISSN: 0175-7571
    Electronic ISSN: 1432-1017
    Topics: Biology , Physics
    Published by Springer
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