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Is the many foldings and twists resulting from the interactions of the R group side chains; hydrophobic interactions, hydrogen bonding between polar groups, ionic bonding between charged groups, hydrophyllic interactions and covalent bonding between sulfur containing groups. All this contributes to the globular or other shape the mature protein will take.
The R groups of the amino acids in its active site
Ultimately, the unique sequence of amino acids making up the primary polypeptide chain. The R group interactions give the protein it's tertiary shape.
There are 20 R Groups, just like there is 20 Amino acids.
Hybrids
This is not in the primary structure, or even from the primary structure. This folding of proteins into the globular final shape by the bonding interaction of R groups is called the tertiary phase of protein synthesis. ( tertiary means three )
They give them their shape.
Is the many foldings and twists resulting from the interactions of the R group side chains; hydrophobic interactions, hydrogen bonding between polar groups, ionic bonding between charged groups, hydrophyllic interactions and covalent bonding between sulfur containing groups. All this contributes to the globular or other shape the mature protein will take.
The bases of the various amino acids are hydrogen bonded in the secondary structure of protein synthesis. Alpha helices and beta sheets are formed. This is the step before the various R groups start bonding and folding the protein into a globular shape in the tertiary structure.
A change in pH can alter the ionization of the R groups of the amino acids. When the charges on the amino acids change, hydrogen bonding within the protein molecule changes and the molecule changes shape. The new shape therefore may not be effective
The first level
Because each amino acid put into the growing polypeptide chain that will become a protein has an R group with different binding characteristics that can change the shape of the protein, thus the action of the protein, if not accurately placed for that particular protein in it's tertiary form.
The R groups of the amino acids in its active site
A protein's structure is determined by:- the amino acid sequences of its polypeptide chains;- hydrogen bonds between amino acids in polypeptides;- other bonds (e.g. hydrophobic interactions, disulphide bridges) between side chains in the polypeptides; and- the arrangement of polypeptides (in a protein that contains more than one polypeptide)Scientists have mapped the structures of several proteins; however, scientists are still unsure as to how proteins actually form their final structures.The function of a protein is directly related to its structure. For example, a protein that fights a certain bacteria might have a shape that allows it to bind to the bacteria and then destroy it.
Ultimately, the unique sequence of amino acids making up the primary polypeptide chain. The R group interactions give the protein it's tertiary shape.
When a protein is denatured it involves the disruption and possible destruction of both tertiary and secondary structures. The denature of proteins can happen through the exposure of chemicals or heat.
The answer will depend on what the shape is and which aspect of the shape is measured by r.