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  • Circular dichroism  (1)
  • Second order initial value problems  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    BIT 27 (1987), S. 599-614 
    ISSN: 1572-9125
    Keywords: MAS ; 65L05 ; Second order initial value problems ; oscillation problems ; efficientP-stable methods
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract In this paper, a family of fourth orderP-stable methods for solving second order initial value problems is considered. When applied to a nonlinear differential system, all the methods in the family give rise to a nonlinear system which may be solved using a modified Newton method. The classical methods of this type involve at least three (new) function evaluations per iteration (that is, they are 3-stage methods) and most involve using complex arithmetic in factorising their iteration matrix. We derive methods which require only two (new) function evaluations per iteration and for which the iteration matrix is a true real perfect square. This implies that real arithmetic will be used and that at most one real matrix must be factorised at each step. Also we consider various computational aspects such as local error estimation and a strategy for changing the step size.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1017
    Keywords: Key wordsα-helical coiled coil ; Sedimentation equilibrium ; Circular dichroism ; Peptide and protein self-association
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Alpha-helical coiled coils are proving to be almost ideal systems for the modelling of peptide and protein self-association processes. Stable oligomeric systems, in which the stoichiometry is well defined, can be produced by the careful selection of the appropriate amino acid sequence, although the principles behind this are still not fully understood. Here we report on a 35 residue peptide, FZ, synthesized by the solid phase method, which was originally designed to form a dimer, but which, in fact, associates to the trimeric state. A detailed characterization of the associative properties of the peptide has been performed by circular dichroism spectroscopy and, in particular, by sedimentation equilibrium in the analytical ultracentrifuge. The presence of the trimeric state, which is stable even at low peptide concentrations, has been confirmed by various, independent methods of analysis for molar mass. The effects of both temperature and of guanidinium chloride on the peptide have been investigated and both found to be peptide-concentration dependent. The unfolding induced by the denaturant cannot be adequately described by a simple, two state monomer-trimer equilibrium.
    Type of Medium: Electronic Resource
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