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  • 1
    Electronic Resource
    Electronic Resource
    Theory of protein molecule self-organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 469-495 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: This paper presents the results of a stereochemical analysis of local interactions in unfolded protein chains (sterical repulsions, hydrogen, and hydrophobic bonds, etc.) by means of space-filling modeles. On the basis of this analysis, an evaluation is made of thermodynamic parameters controlling the building-in of all the 20 natural amino acid residues in all the physically possible position of local secondary structures (α-helices, including α-helices with short fragments of helices 310 at the C-terminus; β-bends of different types, helices 310, and their combinations) as well as thermodynamic parameters of separate hydrogen bonds of polar side groups with the neighbor peptide groups (“local contacts”). The accuracy of the obtained results is discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160302
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  • 2
    Electronic Resource
    Electronic Resource
    Mechanism of protein folding (1979)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 16 (1979), S. 407-418 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The first stage of protein self-organization - the formation of a fluctuating secondary structure in the unfolded protein chain - is considered. The stereochemical theory is presented enabling one to calculate helix-coil and β-structure-coil equilibrium constants. It is shown that the most probable localization of fluctuating α- and β-structure in the unfolded protein chain corresponds to the native localization of these structures. The formation of large α- and β-structural blocks is observed, each of them including several native α-helices or β-strands.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560160302
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  • 3
    Electronic Resource
    Electronic Resource
    Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 497-524 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Constants of the helix-coil transition for all natural amino acid residues are evaluated on the basis of thermodynamic parameters obtained in paper I of this series. The specific effects at the termini of the helices are also considered as well as the parameters controlling the formation of β-bends in the unfolded protein chain. Evaluated s constants of the helix-coil transition agree with the experimental data on helix-coil transitions of synthetic polypeptides in water. Only a very qualitative correlation exists between s constants (both experimental and theoretical) and the occurrence of corresponding residues in internal turns of α-helices in globular proteins: residues with s 〉 1 occur in helices as a rule more often than residues with s 〈 1. At the same time a direct correlation is demonstrated between theoretical parameters of residue incorporation into α-helical termini and β-bends in an unfolded polypeptide chain and the occurrence of residues in corresponding positions of the globular protein secondary structures.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160303
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  • 4
    Electronic Resource
    Electronic Resource
    Thermodynamic parameters of the helix-coil transition in polypeptide chains. III. Random copolymers of L-leucine with L-glutamic acidThe preceding two papers of this series are Refs. 1 and 2. (1975)
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 1739-1753 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Conformational transitions induced by pH changes in random copolymers of leucine and glutamic acid have been studied. Significant differences were observed in the potentiometric titration curves of copolymers with small (up to 4%) and large leucine contents. The helical stability of copolymers with small leucine content, determined from titration curves by the Zimm and Rice method, decreases slightly with an increase in the leucine content, whereas the helical stability of copolymers with large leucine content increases sharply with an increase of the leucine content. It is shown that copolymers with large leucine content aggregate in the region of transition into the helical state, but the increase of their helical state stability is not connected with intermolecular aggregation, as it was also observed for a nonaggregating fraction isolated from one of the copolymers by gel chromatography. A conclusion is made that the helix-coil equilibrium constant s for leucine does not itself exceed the s constant for uncharged polyglutamic acid. The stabilization of the helical state in copolymers with large leucine content is due to intramolecular aggregation of helices in these copolymers. The analysis of the leucine residue distribution between helical and nonhelical regions in globular proteins also gives no real arguments to ascribe special helix-forming properties to leucine.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1975.360140814
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