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  • Polymer and Materials Science  (18)
  • EARTH RESOURCES AND REMOTE SENSING  (15)
  • 1
    Electronic Resource
    Electronic Resource
    Microdomain dynamics in folding proteins (1982)
    New York : Wiley-Blackwell
    Biopolymers 21 (1982), S. 1275-1300 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The basic formulas for the incorporation into the diffusion-collision model of the stabilities of intermediate states on the folding pathway are derived and discussed. A hypothetical two-step folding pathway is calculated in detail. A model for the production of incorrectly folded intermediates is suggested and some numerical estimates made. Implications and future directions in the evolution of the model are discussed. Three appendices deal with some mathematical aspects of the model.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360210703
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  • 2
    Electronic Resource
    Electronic Resource
    Alternative pathways in diffusion-collision controlled protein folding (1984)
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 675-694 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The diffusion-collision model of protein folding has been solved exactly for a three-microdomain protein subunit. Numerical analysis shows that the exact kinetics may be excellently approximated in all cases studied by a standard chemical kinetics approach with the forward rate constants calculated from the mean folding time formula found previously.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360230408
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  • 3
    Electronic Resource
    Electronic Resource
    Brownian dynamics simulation of protein folding: A study of the diffusion-collision modelSupported in part by a grant from the National Science Foundation. (1987)
    New York : Wiley-Blackwell
    Biopolymers 26 (1987), S. 481-506 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The dynamic aspects of protein folding are described by a series of diffusion-collision steps involving structural units (microdomains) of various sizes that combine to form the protein in its native state. A method is introduced for obtaining the rate constants for the basic diffusion-collision step by use of Brownian dynamics. The method is applied to an investigation of the folding dynamics of two α-helices connected by a flexible (random-coil) polypeptide chain. The results of this full three-dimensional treatment are compared with simplified model calculations for the diffusion-collision step. Of particular interest are the nature of the collision dynamics and the role of the intervening peptide chain.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360260404
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  • 4
    Electronic Resource
    Electronic Resource
    Relation between calculated amide frequencies and solution structure in Ala-X peptidesThe opinions or assertions contained herein are the private ones of the authors and are not to be construed as official or reflecting the views of the U.S. Department of Defense or the Uniformed Services University of the Health Sciences. (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 599-608 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Computational techniques have been used to aid interpretation of observed systematic shifts in the amide III frequencies of Ala-X peptides. Optimized structures and frequencies have been calculated for Ala-X peptides using GAUSSIAN86/88 with the 4-31G basis, MOPAC, and normal mode methods based on empirical force fields. We observe the following: (1) Frequencies calculated using scaled GAUSSIAN86 force constants correlate well with the experimental results. (2) Structures of the Ala-X peptides optimized by GAUSSIAN show a clear trend toward lower values of the dihedral angle φ as the X side chain becomes larger, while structures optimized here using semiempirical and empirical force fields do not show trends. (3) Computational changes in peptide conformations from β-sheet to α-helix produce large changes in both amide I and amide III frequencies that are inconsistent with the experimental results. (4) Computational changes in the dihedral angle φ of Ala-Ala produce a change in the amide III frequency consistent with the experimental results. (5) The experimental frequency shifts cannot be attributed directly to the effects of changing mass.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300512
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  • 5
    Electronic Resource
    Electronic Resource
    Simulation of α-helix-coil transitions in simplified polyvaline: Equilibrium properties and brownian dynamics (1993)
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 1519-1535 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A quantitative understanding of helix-coil dynamics will help explain their role in protein folding and in folded proteins. As a contribution to the understanding, the equilibrium and dynamical aspects of the helix-coil transition in polyvaline have been studied by computer simulation using a simplified model of the polypeptide chain. Each amino acid residue is treated as a single quasiparticle in an effective potential that approximates the potential of mean force in solution. The equilibrium properties examined include the helix-coil transition and its dependence on chain position and well depth at the coil-helix interface. A stochastic simulation of the Brownian motion of the chain in its solvent surroundings has been used to investigate dynamical properties. Time histories of the dihedral angles have been used to study the behavior of the helical structure. Auto and cross-correlation functions have been calculated from the time histories and from the state (helix or coil) functions of the residues with relaxation times of tens to hundreds of picoseconds. Helix-coil rate constants of tens of ns-1 were found for both directions of the transition. © 1993 John Wiley & Sons, Inc.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360331004
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  • 6
    Electronic Resource
    Electronic Resource
    Stress-strain properties of rubber at pressures above the glass transition pressure (1969)
    New York : Wiley-Blackwell
    Journal of Polymer Science Part A-2: Polymer Physics 7 (1969), S. 587-592 
    Details
    ISSN: 0449-2978
    Keywords: Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pol.1969.160070312
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  • 7
    Electronic Resource
    Electronic Resource
    Weighted intrinsic viscosity relationships for polysaccharide mixtures in dilute aqueous solutions (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 35 (1988), S. 1631-1637 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: The weighted intrinsic viscosities of polysaccharide mixtures in dilute aqueous solutions have been studied. The purpose of this investigation is to demonstrate that average intrinsic viscosities would scale with the weight fraction of the individual components for polysaccharide mixtures in 0.5N NaOH(aq). The polysaccharides examined in this study were composed of polymers differing in their molecular weights, degree of branching, and bond linkages. Excellent agreement between theory and experiment was observed for the three different mixed polymer systems examined. This observation validates certain aspects of proposed theoretical treatments which employ this fundamental assumption and allows for further advances in experimental analytical developments of water-soluble polymer systems.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1988.070350618
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  • 8
    Electronic Resource
    Electronic Resource
    Amide III frequencies for Ala-X peptides depend on the X amino acid sizeThe opinions or assertions contained herein are the private ones of the authors and are not to be construed as official or reflecting the views of the U.S. Department of Defense or the Uniformed Services University of the Health Sciences. (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 593-597 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Raman spectra of series of aqueous solutions of peptides containing two amino acids, glycine-X, alanine-X, and serine-X, where X is an uncharged amino acid, show that the amide III band shifts systematically to lower frequencies as the side chain of the X amino acid becomes larger. The range of this shift is about 20cm-1, starting at 1275cm-1 for alanine-glycine and moving to 1251 cm-1 for alanine-tryptophan, with a correlation coefficient of 0.93 with the mass of the X amino acid side chain for 10 peptides. The amide I frequencies remain constant as the X amino acid is changed. This shift may result from a change in the average conformational preference of the peptide, a change in vibrational coupling of the amide III modes with the X amino acid side chain, a change in molecular force constants, or a combination of these. These results present a test for computational methods.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300511
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  • 9
    Electronic Resource
    Electronic Resource
    Diffusion-collision model for protein folding (1979)
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 1421-1437 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The basic equations for the elementary step in the diffusion-collision-coalescence model of protein folding are derived for the case of two radially diffusing spherical microdomains. Refinements and biological implications of the mechanism are considered; included are detailed discussions of the parameters of the model, the possibilities of rotational diffusion and surface diffusion in one or two dimensions, the nature of the microdomains, and the application of the model to protein unfolding.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1979.360180608
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  • 10
    Electronic Resource
    Electronic Resource
    Hydrophobic interaction between globin helices (1992)
    New York : Wiley-Blackwell
    Biopolymers 32 (1992), S. 477-490 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The interhelical interfaces have been examined in seven high-resolution globin chains. The profiles of hydrophobic contact, as measured by the residue solvent-accessible area loss upon folding, have been calculated. The seven globins studied differ in their overall loss of solvent-accessible area upon packing of their helices, the order being 1MBD 〉 1LH1 〉 1ECD 〉 2MHBB 〉 2HHBB 〉 2HHBA 〉 2MHBA, which gives a measure of the difference in stability due to the hydrophobic interaction. The five helix-pair packings (AH, BE, BG, FH and GH) examined in detail have qualitative similarities. There are, however, substantial quantitative differences both at the equivalent residue level and at the level of overall helix-helix contact, which has significance in some models of folding. The AH pair has the most uniform area loss over the seven globins and the largest variation in accessible area loss on packing among the five helix pairs is the GH pair. The set of residues required to produce the globin fold has been deduced from the residue area losses.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360320504
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