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I noticed that most disulfide bonds occur when two cysteine side chains exist in close proximity to each other. Do those cysteine side chains "look out" for each other during folding, that is do they cause the polypeptide to fold so that a disulfide bond can be formed? If not, does this mean that they contribute to the tertiary structure of the polypeptide by stabilising only?

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    $\begingroup$ I do not suppose SH groups have abilities to look for each other. They are brought together to bond themselves by protein forming mechanisms, probably in ribosoms. What does not exclude incidental bonding. $\endgroup$
    – Poutnik
    Aug 17, 2022 at 8:01
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    $\begingroup$ The introduction and conclusion of this paper contains relevant information and citations, including the classic Anfinsen work. $\endgroup$
    – Karsten
    Aug 17, 2022 at 10:50

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