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What are the weak interactions that govern the tertiary structure of proteins?
Wiki User
∙ 14y ago
As you know that hydrogen bonding aids the formation of the secondary structures. Once these structures are formed (ie alpha helix, beta-sheet, beta-turn), the R groups now can interact with other R groups. In the tertiary structure, the weak interactions (ie hydrogen bonding, ionic bonding, van der waals interactions) aid in the 3D structure of the protein. Disulfide bonds form in the tertiary structure which add extra stability to the overall 3D shape of the protein.
good luck.
Wiki User
∙ 13y ago
Wiki User
∙ 9y agoA globular protein's secondary and tertiary structure is highly dependent on a variety of stabilizing forces. Many of the most critical structural features are hand in place by little more than a few hydrogen bonds. Disulfide bonds are stronger, but are generally required to hold larger folds close.
Wiki User
∙ 14y agoThe tertiary structure of proteins is decided by the nature of the parts of the protein, the amino acids.
Amino acids can be negative, positive, or neutral. This will exert electrostatic effects (weak interactions) on the amino acids around it, like magnets pulling or pushing each other away depending on their orientation. Neutral amino acids tend to clump together and form the cores of proteins, but this is not always the case.
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