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Dictionary » C » Chaperonins ChaperoninsChaperonins a class of sequence-related molecular chaperones found in bacteria, mitochondria, and plastids. Chaperonins are abundant constitutive proteins that increase in amount after stresses such as heat shock, bacterial infection of macrophages, and an increase in the cellular content of unfolded proteins. Bacterial chaperonins are major immunogens in human bacterial infections because of their accumulation during the stress of infection. Two members of this class of chaperones are chaperonin 10 and chaperonin 60. ![]()
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Results from our forumRe: Re:... statement, that is very wrong. Creative errors are common. Just see simple mutations giving rise to antibiotic resistance. Gene duplications, chaperonins and other mechanism allow the accumulation of mutations without effects, until an event disturb the balance. And generally bad mutations ...
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Theoretical biologists developing a protein folding theory?... folding of protein happens in 3 ways, (1) it folds by itself, (2) helped by proteins named chaperones, and (3) helped by a large dome-like protein chaperonins. for the no.1, it can fold to a proper structure sometimes because of series of actions happened after translation, called post-translational ...
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Polypeptides... polypeptides are often modified in Golgi by attaching oligosaccharides. When polypeptides emerge from polyribosomes, they often are caught by chaperonins which help polypeptides fold into their tertiary structure. These folded polypeptides can unite one with other to form a multi-polypeptide ...
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the puzzle of chaperones!... chaperones as a 'guide' to help them fold.. I do realise that most proteins also can fold themselves without the help of chaperones (Hsp 70) or chaperonins (Hsp 60).. but the question is how do chaperones or chaperonins themselves manage to fold in the correct order? i do realise that maybe ...
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