"... In PAGE 4: ... 7). Bacterial magnetic particles at successive dendrimer generations were investigated for DNA binding abilities ( Table1 ). The amine numbers double with every layer generated on the BMP surface.... ..."

"... In PAGE 46: ... In general, energy minimizations for the unsolvated peptide indicate an enormous number of local minima which represent metastable structures corresponding to partially right{hand and left{hand {helices. In initializing the algorithm the information in Table3 provides 4 initial regions for each glycine residue, or a total of 104 initial subdomains for the entire decapeptide. This was modi ed to 32 initial subdomains by combining the subdomains for each residue, and searching the entire space (-180,180) for every other glycine residue.... ..."

"... In PAGE 12: ... Additional evidence was gained by observing loss of the migratory band associated with the dendrimer core reagent present in the ini- tial reaction mixture, accompanied by the formation of a higher molecular weight product, which dis- played a much shorter migratory band position on the electrophoretic gel. In fact, the molecular weights of the resulting core-shell tecto(dendrimer) could be estimated by comparing the migratory time of the core-shell product (PAGE results, Table1 ) with the migration distances of the PAMAM dendrimers (e.... In PAGE 12: ...bserved for 1:1 reaction ratios described in our earlier work [39] in this report (Fig. 11). Molecular weights for the final products were determined by MALDI-TOF-MS or (polyacry- lamide) gel electrophoresis (PAGE). They were corroborated by calculated values from AFM dimen- sion data ( Table1 ) and were found to be in relatively good agreement within this series (Table 1). Calculations based on these experimentally determined molecular weights allowed the estimation of shell filling levels for respective core-shell structures within this series.... ..."

"... In PAGE 14: ... Table 4 shows the P-values of the amino acids at each of the sixteen linker positions. In Table4 and Figure 9 the amino acids have been roughly grouped according to the attributes hydrophobic, charged, and polar (following the classification of Branden and Tooze83). As shown in Table 4 and Figure 9, the frequencies of the remaining amino acids in linkers are not statistically different from the database as a whole at the 5% significance level.... In PAGE 14: ... In Table 4 and Figure 9 the amino acids have been roughly grouped according to the attributes hydrophobic, charged, and polar (following the classification of Branden and Tooze83). As shown in Table4 and Figure 9, the frequencies of the remaining amino acids in linkers are not statistically different from the database as a whole at the 5% significance level. The statistical significance of the results of the computed amino acid averages can be assessed by comparing the composition of the linker sequences with random data sets of Table 3.... ..."

"... In PAGE 14: ... Table 4 shows the P-values of the amino acids at each of the sixteen linker positions. In Table4 and Figure 9 the amino acids have been roughly grouped according to the attributes hydrophobic, charged, and polar (following the classification of Branden and Tooze83). As shown in Table 4 and Figure 9, the frequencies of the remaining amino acids in linkers are not statistically different from the database as a whole at the 5% significance level.... In PAGE 14: ... In Table 4 and Figure 9 the amino acids have been roughly grouped according to the attributes hydrophobic, charged, and polar (following the classification of Branden and Tooze83). As shown in Table4 and Figure 9, the frequencies of the remaining amino acids in linkers are not statistically different from the database as a whole at the 5% significance level. The statistical significance of the results of the computed amino acid averages can be assessed by comparing the composition of the linker sequences with random data sets of Table 3.... ..."

"... In PAGE 11: ... To check whether some of these sites are conserved between multiple organisms, we map them on the alignment of orthologous protein. 37 proteolytic sites are found conserved between two or more organisms (see Table3 ). This is a significantly larger number of conserved sites than expected by chance.... ..."