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How does the 3d atomic molecular structure of a beta-strand differ to that of a coil?

I am not interested in comparison with a whole beta-sheet but rather a single beta-strand to a single coil of equal length and equal sequence.

For example, what would be the difference between the folded and unfolded state, assuming they both form an equal line/curve topology?

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    $\begingroup$ We can explain the structure of a beta-strand to you, but at the moment the rest of your question does not make sense. In protein secondary structure "coil' is short for "random coil". In the DSSP classification it is defined as "residues which are not in any of the above (i.e. recognized secondary structure) conformations". And the "unfolded state" of any protein structure is a random coil. Are you thinking that the unit of a "coiled coil" is a "coil"? It is actually an alpha-helix. Is that what you wish to compare? $\endgroup$ – David Feb 10 at 10:28

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