Search Results - (Author, Cooperation:E. Chun)

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  1. 1
    W. Liu ; E. Chun ; A. A. Thompson ; P. Chubukov ; F. Xu ; V. Katritch ; G. W. Han ; C. B. Roth ; L. H. Heitman ; I. J. AP ; V. Cherezov ; R. C. Stevens
    American Association for the Advancement of Science (AAAS)
    Published 2012
    Staff View
    Publication Date:
    2012-07-17
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Adenosine A2 Receptor Agonists/metabolism ; Adenosine A2 Receptor Antagonists/metabolism ; Allosteric Regulation ; Cholesterol/chemistry ; Crystallography, X-Ray ; Cytochrome b Group/chemistry ; Escherichia coli Proteins/chemistry ; HEK293 Cells ; Humans ; Hydrogen Bonding ; Ligands ; Lipid Bilayers ; Lipids/chemistry ; Models, Molecular ; Protein Conformation ; Protein Engineering ; Protein Structure, Secondary ; Receptor, Adenosine A2A/*chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sodium/*analysis ; Triazines/metabolism ; Triazoles/metabolism ; Water/chemistry
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    Publication Date:
    2012-05-19
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Binding Sites ; Biomimetic Materials/*chemistry/metabolism/pharmacology ; Crystallography, X-Ray ; HEK293 Cells ; Humans ; Ligands ; Models, Molecular ; Narcotic Antagonists ; Opioid Peptides/*chemistry/metabolism/pharmacology ; Piperidines/*chemistry/*metabolism/pharmacology ; Protein Conformation ; Receptors, Opioid/*chemistry/*metabolism ; Receptors, Opioid, kappa/chemistry/metabolism ; Spiro Compounds/*chemistry/*metabolism/pharmacology ; Substrate Specificity
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  3. 3
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  5. 5
    Sui Chun-e
    Institute of Physics (IOP)
    Published 2018
    Staff View
    Publication Date:
    2018-06-03
    Publisher:
    Institute of Physics (IOP)
    Print ISSN:
    1755-1307
    Electronic ISSN:
    1755-1315
    Topics:
    Geography
    Geosciences
    Physics
    Published by:
    Latest Papers from Table of Contents or Articles in Press
  6. 6
    Staff View
    ISSN:
    1573-4943
    Keywords:
    Triple helix ; fibril ; coiled-coil ; telopeptide ; cross-linking, molecular modeling
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Chemistry and Pharmacology
    Notes:
    Abstract An energy minimized three-dimensional structure of a collagen microfibril template was constructed based on the five-stranded model of Smith (1968), using molecular modeling methods and Kollman force fields (Weiner and Kollman, 1981). For this model, individual molecules were constructed with three identical polypeptide chains ((Gly-Pro-Pro) n , (Gly-Prop-Hyp) n , or (Gly-Ala-Ala) n , wheren=4, 12, and 16) coiled into a right-handed triple-helical structure. The axial distance between adjacent amino acid residues is about 0.29 nm per polypeptide chain, and the pitch of each chain is approximately 3.3 residues. The microfibril model consists of five parallel triple helices packed so that a left-handed superhelical twist exists. The structural characteristics of the computed microfibril are consistent with those obtained for collagen by X-ray diffraction and electron microscopy. The energy minimized Smith microfibril model for (Gly-Pro-Pro)12 has an axial length of about 10.2 nm (for a 36 amino acid residue chain), which gives an estimated D-spacing (234 amino acids per chain) of approximately 66.2 nm. Studies of the microfibril models (Gly-Pro-Pro)12, (Gly-Pro-Hyp)12, and (Gly-Ala-Ala)12 show that nonbonded van der Waals interactions are important for microfibril formation, while electrostatic interactions contribute to the stability of the microfibril structure and determine the specificity by which collagen molecules pack within the microfibril.
    Type of Medium:
    Electronic Resource
    URL:
    Articles: DFG German National Licenses