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  • Electronic Resource  (3)
  • computer simulation  (2)
  • Key words: Ramachandran map – Protein structure – Molecular modeling – Conformational analysis  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Modelling of transmembrane α-helix bundles (1995)
    Springer
    Molecular engineering 5 (1995), S. 1-9 
    Details
    ISSN: 1572-8951
    Keywords: Protein structure ; computer simulation ; membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A strategy for modelling transmembrane α-helix bundles has been investigated. Results concerning the rotational orientations of the helices are described and perspectives for extensions of the method are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00999574
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Perspective on “Stereochemistry of polypeptide chain conformations” (2000)
    Springer
    Theoretical chemistry accounts 103 (2000), S. 257-258 
    Details
    ISSN: 1432-2234
    Keywords: Key words: Ramachandran map – Protein structure – Molecular modeling – Conformational analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract. Despite its apparent simplicity the “Ramachandran map” has been an enormously successful tool for describing and understanding protein structure. Thirty-five years after its invention, it is still used daily for checking the quality of experimental and modeled protein structures. It is, moreover, founded on a rational, reduced-coordinate model of the polypeptide chain which continues to be useful in computational attempts at predicting protein folding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002149900022
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  • 3
    Electronic Resource
    Electronic Resource
    Packing and recognition of protein structural elements: A new approach applied to the 4-helix bundle of myohemerythrin (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 15 (1993), S. 413-425 
    Details
    ISSN: 0887-3585
    Keywords: computer simulation ; side chain conformations ; optimization ; α-helices ; tertiary structure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We present a novel search strategy for determining the optimal packing of protein secondary structure elements. The approach is based on conformational energy optimization using a predetermined set of side chain rotamers and appropriate methods for sampling the conformational space of peptide fragments having fixed backbone geometries. An application to the 4-helix bundle of myohemerythrin is presented. It is shown that the conformations of the amino acid side chains are largely determined at the level of helix pairs and that superposition of these results can be used to construct the full bundle. The final solution obtained, taking into account restrictions due to the lateral amphiphilicity of the helices, differs from the native structure by only a 20° rotation of a single helix. © 1993 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340150408
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    Paper (German National Licenses)
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