Tums

As stated above the SQUID amplifier demands a low inductance Eddy current probe in order to be able to amplify signals up to 1 MHz. Low inductance Eddy current probes can be obtained by reducing the number of turns and by loosing the magnetic coupling between the tums. So magnetic cores should be avoided as well as tight wounded tums. For this purpose planar coils are the best... 

M. Hochbruck and Ch. Lubich. A bunch of time integrators for quan-tum/classical molecular dynamics, this volume. 

At initial tum-on, the inversion charge = 0 and when n is small and Cj is large, = ca V, that is, a potential well of nearly lAis formed. Thus, the charge-handling capacity, is... 

Figure 8.18 The subunit of the trp repressor. The subunit contains 107 amino acid residues that are folded into six a helices. Helices 4 (blue) and 5 (red) form the DNA-binding helix-tum-helix motif. (Adapted from R.W. Schevitz et ah. Nature 317 782-786, 1985.)...

Figure 8.21 Richardson-type diagram of the structure of one suhunit of the lac repressor. The polypeptide chain is arranged in four domains, an amino terminal DNA-hinding domain (red) with a helix-tum-helix motif, a hinge helix (purple), a large core domain which has two subdomains (green and hlue) and a C-terminal a helix. (Adapted from M. Lewis et al.. Science 271 1247-1254, 1996.)...

Many biochemical and biophysical studies of CAP-DNA complexes in solution have demonstrated that CAP induces a sharp bend in DNA upon binding. This was confirmed when the group of Thomas Steitz at Yale University determined the crystal structure of cyclic AMP-DNA complex to 3 A resolution. The CAP molecule comprises two identical polypeptide chains of 209 amino acid residues (Figure 8.24). Each chain is folded into two domains that have separate functions (Figure 8.24b). The larger N-terminal domain binds the allosteric effector molecule, cyclic AMP, and provides all the subunit interactions that form the dimer. The C-terminal domain contains the helix-tum-helix motif that binds DNA. 

Some of the procaryotic DNA-binding proteins are activated by the binding of an allosteric effector molecule. This event changes the conformation of the dimeric protein, causing the helix-tum-helix motifs to move so that they are 34 A apart and able to bind to the major groove. The dimeric repressor for purine biosynthesis, PurR, induces a sharp bend in DNA upon binding caused by insertion of a helices in the minor groove between the two... 

Harrison, S.C., Aggarwal, A.K. DNA recognition by proteins with the helix-tum-helix motif. Anna. Rev. Biochem. 59 933-969, 1990. 

Fi re 9.9 Comparison of the hellx-tum-helix motifs in homeodomains (a) and X repressor (b). The recognition helix (red) of the homeodomain is longer than in the procaryotic repressor motif. In addition the first helix of the homeodomain [(green in (a)] is oriented differently. 

MOMEN- TUM BALANCE Rate of change of momentum per unit volume Rale of change of momenium by convection per unit volume Rale of change of momentum by molecular transfer (viscous transfer) per volume Generation per volume (External forces) (Ex gravity) Empirically determined flux specified (3)< Velocity specified (1.2b) ... 

Fach-ordnung, /. classification, -schule, /. technical school, special school, -schrift(en)-tum, n. technical literature, -sprache, /. technical language, professional terminology, fach-sprachlich, adv. in technical language. 

---