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Protein molecules that assist in the proper folding that keeps the new polypeptide segregated from "bad influences" in the cytoplasmic environment while it folds spontaneously.
Chaperonins
A chaperone protein is used in the cell to ensure proper protein folding, among other cellular functions.
Ni, just peptide bonding. Hydrophobic interactions do not have significance to folding until tertiary structure folding.
Chaperonins provide a good environment to facilitate protein folding.
The tertiary structure is the folding
Translation and transcription. Then they go into protein folding.
Protein molecules that assist in the proper folding that keeps the new polypeptide segregated from "bad influences" in the cytoplasmic environment while it folds spontaneously.
Rough endoplasmic reticulum.Rough endoplasmic reticulumB.Rough endoplasmic reticulum
The secondary genetic code is the folding of protein.
Chaperonins
A chaperone protein is used in the cell to ensure proper protein folding, among other cellular functions.
Secondary structure. The coiling is the formation of the alpha helix. The folding is the formation of the beta sheets.
NUCLEUS FUNCTION-Protein translocation, folding and transport or protein.
I don't have a clue, what do you think?
The rough ER is the site of protein modification and folding of proteins, if they need folding. The smooth ER is the site of lipid and steroid synthesis.
The rough ER is the site of protein modification and folding of proteins, if they need folding. The smooth ER is the site of lipid and steroid synthesis.