In the context of the present elaboration, different synthetic cystin-knots were introduced in collagenmodelpeptides and their biophysical and structural influences in relation to their position and mode on the collagen triple helix were elucidated. For this purpose a new strategy for the regioselective disulfide assignment for especially strong aggregating peptide chains had to be developed. Furthermore, the influence of different 4-fluoroprolines in the sequence of the alpha-chains on the formation and stability of the triple helix was also analysed.
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In the context of the present elaboration, different synthetic cystin-knots were introduced in collagenmodelpeptides and their biophysical and structural influences in relation to their position and mode on the collagen triple helix were elucidated. For this purpose a new strategy for the regioselective disulfide assignment for especially strong aggregating peptide chains had to be developed. Furthermore, the influence of different 4-fluoroprolines in the sequence of the alpha-chains on the form...
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