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Helix growth

Figure 2. Kinetics of helix growth at different quenching temperatures a) T = 10°C b) T = 20.5 0 c) T = 26.5 C d) T = 28°C (C = 4.7 %3cm" ). In figure 2-a, time is given in a linear scale, in hours. In figure 2-b, time is in a logarithmic scale, up to 10 hours. The continuous line is calculated using eq. (2), the dotted line is calculated using eq. (3). Figure 2. Kinetics of helix growth at different quenching temperatures a) T = 10°C b) T = 20.5 0 c) T = 26.5 C d) T = 28°C (C = 4.7 %3cm" ). In figure 2-a, time is given in a linear scale, in hours. In figure 2-b, time is in a logarithmic scale, up to 10 hours. The continuous line is calculated using eq. (2), the dotted line is calculated using eq. (3).
Supramolecular structure. The observation of the supramolecular structure is of a primary importance both for elucidating the mechanisms of helix growth and defining the parameters of the network. [Pg.216]

Sedimentation coefficient Equilibrium constant for helix growth... [Pg.803]

At very low concentrations (<0.1%) intramolecular bonds are formed preferentially by back folding of the single chains. At concentrations above 1% the helix growth induces chain association and three-dimensional network formation. For that purpose two subsequent processes are involved a) the formation of single helix nuclei and b) aggr ation of these single helices to a triple helix. It appears that the extent and manner of reversion to the collagen fold (triple helix) structure is dq)endent on solvent, temperature and concentration. [Pg.173]


See other pages where Helix growth is mentioned: [Pg.108]    [Pg.211]    [Pg.215]    [Pg.222]    [Pg.143]    [Pg.437]    [Pg.332]    [Pg.103]    [Pg.332]    [Pg.370]    [Pg.58]    [Pg.92]    [Pg.94]    [Pg.234]    [Pg.235]    [Pg.254]    [Pg.267]    [Pg.262]    [Pg.194]   


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