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
    Electronic Resource
    Electronic Resource
    Extended x-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 4708-4716 
    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/bi00389a017
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    An unusual copper-uridine octamer: existence in solution and structural study in its auto-built zeolitic network in the solid state (1987)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 109 (1987), S. 380-386 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00236a015
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A general, weighted least-squares method for the evaluation of small-angle X-ray data without desmearing (1978)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 11 (1978), S. 73-79 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: In order to avoid some of the disadvantages associated with the desmearing methods, a procedure has been developed where the smeared, primary, intensity data can be evaluated directly without desmearing. The procedure consists of the following: first, a model depending on a vector of unknowns, x = (x1, ...., xn), is constructed; then, an iterative search is made for the vector x, and a scale factor s, which corresponds to a local minimum in the error square sum based on the primary, slit-smeared, intensity data. The main advantages with the present method are that the comparison between theory and experiment is made directly with the experimental quantity; thus the experimental errors can be considered in this comparison. Furthermore, some of the disadvantages associated with the desmearing methods are avoided; the method is numerically stable and no extrapolations outside the measured angular range are necessary. Several data sets measured at different concentrations and with different, completely arbitrary, primary-beam weighting functions can be considered in the same refinement. The interparticle scattering effect may also be included in the least-squares refinement. The method is general, so that different models can be tested simply by changing only one subroutine of the computer program. It may also be used to evaluate data impaired by other types of resolution errors; for example, effects due to polychromatic radiation or resolution errors in neutron scattering. Two constructed examples of the application of the method are given: (1) the calculation of the dimensions and the molecular weight of particles with a shape which can be approximated with an ellipsoid of revolution; (2) the calculation of the dimensions and electron-density distribution for spherical particles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889878012807
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Small-angle X-ray scattering from solutions of flow-oriented colloidal particles (1980)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 13 (1980), S. 154-162 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The amount of information which can be obtained from a small-angle X-ray experiment can be considerably increased by orienting the solute particles with external forces during the scattering experiment. In this paper it is shown that orientation by flow, for instance through a capillary tube, gives additional information about size, shape, flexibility and rotational diffusion of the particles. The only requirement, in order to obtain flow-oriented samples, is that the solute particles must be relatively large and asymmetric. On the other hand, if the scattering curve is dependent on the flow rate through the capillary, it can immediately be concluded that the solute particles are asymmetric (or they are deformed in the hydrodynamic field). Equations describing the relationship between flow rate, molecular shape and scattered intensity are given, and theoretical intensity patterns for some representative cases are presented. It follows that there is a fundamental difference in scattering patterns for oblate and prolate ellipsoids of revolution. This difference can be used to differentiate between these two cases. Some experimental results obtained using inorganic model colloids are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889880011776
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Small-angle X-ray investigation of the equilibria between copper(II) and glycyl-L-histidylglycine in water solution. A method for analysing polydispersed systems (1974)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 7 (1974), S. 192-199 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Water solutions of copper(II) and glycyl-L-histidylglycine contain a large particle of molecular weight of approximately 9000 and also low-molecular-weight particles with an average molecular weight of 430. This is shown in a small-angle X-ray scattering study at 21° and neutral pH using a Kratky camera. The concentration of copper(II) was 34–72 mM and the molar ratio of peptide to copper was 1.39 to 1. This study further indicates that the particles contain about ten weight per cent water, and their shapes are an oblate ellipsoid of revolution with an axial ratio of 0.2. The scattering data were analysed with a method similar to that of Mittelbach & Porod [Kolloid Z. Z. Polym. (1965). 202, 40–49]. It was assumed that the particles in solution follow a discontinuous size distribution function dependent on two parameters: one associated with the complex formation constants, and the other with the relative weights of the units building up the complexes. That a very large particle exists is in qualitative agreement with a previous electromotive-force study which indicated that a series of large complexes is formed. The presence of such a large particle in the solution is also in agreement with a single-crystal study on the same system. The crystal structure consists of a three-dimensional network which contains 40% disordered water located in channels limited by rings of six dimers of copper and peptide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889874009241
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Small-angle X-ray scattering study of complexes of individual components from E. coli ribosomes (1978)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 11 (1978), S. 487-487 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: As part of a general X-ray scattering study on individual ribosomal components and their specific complexes, this study deals with the proteins S1, S8, S15, S16 and S20, the S4-binding region of 16-S RNA, S4-RNA, as well as the specific complexes 5-S RNA–L18, 5-S RNA–L18–L25 and S4–RNA–S4; the proteins were prepared under non-denaturing conditions. In agreement with the previous X-ray scattering studies (Österberg, Sjöberg, Liljas & Pettersson, 1976; Österberg, Sjöberg & Garrett, 1976a; Österberg, Sjöberg, Garrett & Littlechild 1977), involving the proteins L7/L12, L18, L25 and S4, the present data indicate that the proteins are elongated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889878013679
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Small-angle scattering of chain molecules in a hydrodynamic field. The internal rigidity of double-stranded DNA (1983)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 16 (1983), S. 349-353 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Small-angle X-ray scattering data from flowing solutions of double-stranded calf thymus DNA, in phosphate buffer of pH 6.91 and 0.2 mol dm−3 ionic strength, have been recorded over a velocity-gradient range from zero up to a maximum value of 15300 s−1. In comparison with small-angle X-ray measurements performed on stationary solutions, the method of flowing the solution through a capillary tube provides information regarding the internal flexibility of the macromolecule in solution. All the X-ray data recorded in this work can be explained by a slightly modified bead-spring chain model of DNA, which consists of linear segments filled with touching beads. The segments are joined together at the ends to form a long array with complete flexibility at each joint. The lengths of the segments follow a Gaussian distribution with a root-mean-square length equal to 100 nm. The diameter of each bead is equal to 3.0 nm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889883010523
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    The metal complexes of peptides and related compounds. VII. The crystal structure of bis(6-aminohexanoato)copper(II) dihydrate (1973)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 29 (1973), S. 1136-1141 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567740873004012
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Solution structure of human plasma fibronectin as a function of NaCl concentration determined by small-angle X-ray scattering (1989)
    Springer
    European biophysics journal 17 (1989), S. 5-11 
    Details
    ISSN: 1432-1017
    Keywords: Human plasma fibronectin ; solution structure ; ionic strength ; flexible bead-chain models ; Monte Carlo simulation ; small-angle X-ray scattering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The structure of human plasma fibronectin in 50 mM Tris-HCl buffer, pH 7.4, containing varying concentrations of NaCl, has been investigated using the small-angle X-ray method. Below 0.3 M NaCl the overall structure of the molecule is disc-shaped; at 0 M NaCl the axial ratio of the disc is about 1:7 and between 0.1 M to 0.3 M it is slightly more asymmetric, with an axial ratio of 1:10. At about 0.3 M NaCl there is a reversible transition to a more open structure, and, from 0.3 M up to 1.1 M NaCl the small-angle X-ray data can be explained by models consisting of ensembles of flexible, non-overlapping, bead-chains generated by a Monte Carlo procedure. Within this concentration range there is a gradual increase in the stiffness of the chains, as well as a decrease in bead radius, which indicates that the molecule becomes more open when the NaCl concentration is increased. The transition to a more open structure is also demonstrated by the average radius of gyration which increases gradually from 8.26 nm at 0 M NaCl to 8.75 nm at physiological or near-physiological conditions, and up to 16.2 nm at 1.1 M NaCl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257140
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Characterization of a half-molecular fragment obtained by reduction of human α2-macroglobulin with dithiothreitol (1985)
    Springer
    European biophysics journal 13 (1985), S. 25-30 
    Details
    ISSN: 1432-1017
    Keywords: α2-macroglobulin ; subunit structure ; smallangle X-ray scattering ; small-angle neutron scattering ; supercooling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract A half-molecular fragment of α2-macroglobulin has been prepared by reducing and alkylating the inter-subunit disulfide bonds in the tetrameric α2-macroglobulin molecule with 1 mM dithiothreitol (40 min) and 3 mM iodoacetamide (40 min). Further purification was made by gel chromatography and the homogeneous population of halfmolecules has been characterized by the techniques of small-angle X-ray and neutron scattering. The radii of gyration found by the two methods are 57.0 and 58.0 Å, respectively. The match point, obtained by neutron scattering from solutions with different H2O/D2O rations, is at 43% D2O; the data are consistent with a particle having a higher scattering density at large distances from the particle centre. From the X-ray and neutron intensities scattered at zero angle, the specific volume was determined to be 0.73 cm3/g at+5°C and the molecular weight to be 390,000; the latter value is associated with a relatively large error due to the uncertainty in the concentration determination. Shape analysis indicates that the best-fitting scattering-equivalent threeaxial bodies are oblate shaped, with two of their axial dimensions about three to four times larger than the third one. From the volume of the best-fitting scattering-equivalent three-axial bodies, 0.72×106 Å3, we obtain a water content equal to 0.38 g H2O/g protein (dry weight).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266306
    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...