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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. $\endgroup$ – orthocresol Nov 15 '15 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 Nov 15 '15 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. Nov 15 '15 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 :) $\endgroup$ – Hemes Al Saria Nov 15 '15 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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