Structures secondary gains from

The structural information gained from the analysis of myoglobin served as the basis for hypotheses on tertiary structure. However, myoglobin is an atypical globular protein since it lacks cysteinyl residues (no disulphide bonds) and P-con-formation, but contains a very large proportion of a-helical structure. Studies on over 200 globular proteins have demonstrated that polypeptide chains frequently contain both a-helical and P-sheet secondary structures (Figure 4.16). 

Figure 12.20 shows the structure of the side-window circular cage type and linear focused head-on type of photomultiplier which are both preeminent in fluorescence studies. The lower cost of side-window tubes tends to favor their use for steady-state studies, whereas the ultimate performance for lifetime studies is probably at present provided by linear focused devices. In both types internal current amplification is achieved by virtue of secondary electron emission from discrete dynode stages, usually constructed of copper-beryllium (CuBe) alloy, though gallium-phosphide (GaP) first dynodes have been used to obtain higher gains. 

Conformations of primary, secondary, and tertiary amides of (R,R)-tartaric acid, both symmetrically and asymmetrically substituted, have been studied ciys-tallographically [22, 24, 29, 30-40] Moreover, ab initio studies up to MP2 / 6-31G //RHF/6-31G level [41] for both the diamide and N,N,N ,N -tctramcthyl-diamide of (/ ,/ [-tartaric acid have been carried out [20, 22]. X-ray results have shown that primary and secondary amides of (R,R [-tartaric acid tend to adopt a conformation with the extended carbon chain - the Taa structure. In this Taa conformation both the a-hydroxy-amide moieties form planes and the structure gains stabilization from hydrogen bonding between donors, the NH, and acceptors, the proximal OH groups. Moreover, the Taa structure is favorably stabilized by the attraction of antiparallel local dipoles formed along distal C H and Csp2=0 bonds [18, 21, 22],... 

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