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Structure formation bonding sites

In all cases, these aggregates had a uniform diameter of a few nanometers, that is, on the same length scale as the molecular dimensions. Hence, they appeared to be well-defined supramolecular polymers (rather than micellar or vesicular structures) with the propensity to higher-order structure formation. The exact natureofthelatterwasfoundtodependonthenumberofadditionalN—H G=C type hydrogen-bonding sites in the molecules end groups. [Pg.89]

Figure 2 Details of two successive trans-esterification reactions. In the first step, the 2 -OH group of the branch point adenosine nucleophilically attacks the phosphate at the junction of the S exon and intron (S splice site), resulting in the formation of a new S -2 phosphodiester bond between the first nucleotide of the intron and the branch point adenosine (lariat structure formation) and breakage of an old 3 -S phosphodiester bond between the last nucleotide of the S exon and the first nucleotide of the intron (cut-off S exon formation). In the second step, the 3 -OH group of the cut-off S exon nucleophilically attacks the phosphate at the junction of the intron and 3 exon, ligating the two exons (mRNA formation) and releasing the lariat intron. The phosphates at the S splice site (red) and at the 3 splice site (green) and the branch point adenosine and its 2 -OH group are pictured. The lines represent the intron and boxes depict exons (El and E2). Figure 2 Details of two successive trans-esterification reactions. In the first step, the 2 -OH group of the branch point adenosine nucleophilically attacks the phosphate at the junction of the S exon and intron (S splice site), resulting in the formation of a new S -2 phosphodiester bond between the first nucleotide of the intron and the branch point adenosine (lariat structure formation) and breakage of an old 3 -S phosphodiester bond between the last nucleotide of the S exon and the first nucleotide of the intron (cut-off S exon formation). In the second step, the 3 -OH group of the cut-off S exon nucleophilically attacks the phosphate at the junction of the intron and 3 exon, ligating the two exons (mRNA formation) and releasing the lariat intron. The phosphates at the S splice site (red) and at the 3 splice site (green) and the branch point adenosine and its 2 -OH group are pictured. The lines represent the intron and boxes depict exons (El and E2).
Single Molecule Force Spectroscopy - Force-Distance Measurements Measuring the force as a function of tip-sample distance can yield information on the elasticity of individual supermolecules, on conformational transitions (e.g. of proteins), on the mechanical stability of chemical bonds and secondary structures, as well as of the desorption of the molecules from the solid substrate [82, 92-94]. Moreover, information on the chemical bond formation of the tip cluster with a particular bonding site on the sample surface can be obtained [95]. [Pg.367]


See other pages where Structure formation bonding sites is mentioned: [Pg.174]    [Pg.182]    [Pg.159]    [Pg.120]    [Pg.9]    [Pg.693]    [Pg.111]    [Pg.272]    [Pg.34]    [Pg.124]    [Pg.606]    [Pg.23]    [Pg.90]    [Pg.85]    [Pg.85]    [Pg.86]    [Pg.92]    [Pg.256]    [Pg.735]    [Pg.281]    [Pg.256]    [Pg.232]    [Pg.233]    [Pg.202]    [Pg.93]    [Pg.11]    [Pg.452]    [Pg.258]    [Pg.147]    [Pg.202]    [Pg.207]    [Pg.246]    [Pg.145]    [Pg.5719]    [Pg.62]    [Pg.149]    [Pg.79]    [Pg.92]    [Pg.222]    [Pg.94]    [Pg.101]    [Pg.851]    [Pg.126]    [Pg.367]    [Pg.242]    [Pg.271]    [Pg.297]    [Pg.51]   
See also in sourсe #XX -- [ Pg.33 ]




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Formation, sites

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Site structural

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Structure formation

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