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  • 1
    Electronic Resource
    Electronic Resource
    Small-angle neutron scattering studies on Brij-58 micelles (1988)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 92 (1988), S. 729-732 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100314a029
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin (1981)
    [s.l.] : Nature Publishing Group
    Nature 292 (1981), S. 81-82 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Arrangement of proximal (F8) and distal (E7) histidines in oxyMb. At pH 8.4, nitrogen-bound hydrogen on E7 imidazole can be bonded to either Ne (the naturally predominant form), with a hydrogen bond to O-2 (dotted line), or to N6, where it projects into the solvent surrounding the molecule. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/292081a0
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  • 3
    Electronic Resource
    Electronic Resource
    Binding of Cyclo propane to Sperm Whale Myoglobin (1967)
    [s.l.] : Nature Publishing Group
    Nature 214 (1967), S. 1120-1122 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. (a) h0l difference electron density map ; (b) hk0 difference electron density map. Contours at arbitrary intervals, positive contours full line, negative contours dashed. The zero contour has been omitted. The peak heights in the centric h0l projection (a) are higher than those in the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2141120a0
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  • 4
    Electronic Resource
    Electronic Resource
    Binding of Xenon to Sperm Whale Myoglobin (1965)
    [s.l.] : Nature Publishing Group
    Nature 207 (1965), S. 28-30 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IN 1946 Lawrence et al.1 and Tobias et al.2 suggested that xenon might be expected to have anaesthetic effects in consequence of its relatively large inducible dipole. In 1951 Cullen and Gross3 confirmed that xenon was indeed an anaesthetic agent in man4. The electron cloud of xenon is, of course, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/207028a0
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  • 5
    Electronic Resource
    Electronic Resource
    Neutron Diffraction Analysis of Myoglobin (1969)
    [s.l.] : Nature Publishing Group
    Nature 224 (1969), S. 143-146 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A preliminary analysis of myoglobin proves that neutron diffraction analysis of proteins is feasible and should reveal the position of fixed hydrogen ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/224143a0
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular dynamics simulation of hydration in myoglobin (1995)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 22 (1995), S. 20-26 
    Details
    ISSN: 0887-3585
    Keywords: computer simulation ; molecular dynamics ; bound water ; hydrogen bonds ; neutron analysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: This study was carried out to evaluate the stability of the 89 bound water molecules that were observed in the neutron diffraction study of CO myoglobin. The myoglobin structure derived from the neutron analysis was used as the starting point in the molecular dynamics simulation using the software package CHARMM. After solvation of the protein, energy minimization and equilibration of the system, 50 ps of Newtonian dynamics was performed. This data showed that only 4 water molecules are continously bound during the length of this simulation while the other solvent molecules exhibit considerable mobility and are breaking and reforming hydrogen bonds with the protein. At any instant during the simulation, 73 of the hydration sites observed in the neutron structure are occupied by water. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340220104
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