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I'm learning about mass spectroscopy in particular the use of it in analyzing protein structure. they said we have to use trypsinolysis to cut the protein to segments, but why does the protein have to be denatured first before trypsinolysis?

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    $\begingroup$ This should be on Biology. $\endgroup$ Commented Nov 15, 2015 at 1:24
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    $\begingroup$ I'm voting to close this question as off-topic because it would be more appropriate on biology.SE. $\endgroup$
    – bon
    Commented Nov 15, 2015 at 11:50
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    $\begingroup$ I disagree that this belongs on biology. Enzymes are chemical entities that do chemistry! $\endgroup$
    – Curt F.
    Commented Nov 15, 2015 at 19:07
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    $\begingroup$ I put it as a chemistry question because I'm learning about this on my chemistry course in biomedicine- so thought its more appropriate here :) $\endgroup$ Commented Nov 15, 2015 at 22:23

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Trypsin is an enzyme, and has to bind to a target protein in a specific way in order to be active. Without first denaturing your protein, most of the protein will be conformationally/sterically inaccessible to trypsin, and you will only get partial digestion (or maybe no digestion at all).

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