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Describe the formation of the primary structure and secondary structure of proteins?
Anonymous
more than 3 weeks ago
Describe the formation of the primary structure and secondary structure of proteins?
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ChatGPT
more than 3 weeks ago
The primary structure of a protein is determined by the sequence of amino acids in the polypeptide chain. This sequence is dictated by the genetic code and is encoded in the DNA of the organism. The amino acids are linked together by peptide bonds, forming a linear chain.
The secondary structure of a protein refers to the local folding patterns that occur within the polypeptide chain. The two most common types of secondary structure are alpha helices and beta sheets. Alpha helices are formed when the polypeptide chain twists into a spiral shape, while beta sheets are formed when the chain folds into a pleated sheet-like structure.
The formation of secondary structure is driven by hydrogen bonding between the amino acid residues in the polypeptide chain. In an alpha helix, hydrogen bonds form between the carbonyl group of one amino acid and the amino group of another amino acid, stabilizing the helical structure. In a beta sheet, hydrogen bonds form between adjacent strands of the polypeptide chain, holding the sheet together.
Overall, the primary structure of a protein determines the sequence of amino acids, while the secondary structure refers to the local folding patterns that occur within the polypeptide chain. These structures are essential for the overall shape and function of a protein.
The secondary structure of a protein refers to the local folding patterns that occur within the polypeptide chain. The two most common types of secondary structure are alpha helices and beta sheets. Alpha helices are formed when the polypeptide chain twists into a spiral shape, while beta sheets are formed when the chain folds into a pleated sheet-like structure.
The formation of secondary structure is driven by hydrogen bonding between the amino acid residues in the polypeptide chain. In an alpha helix, hydrogen bonds form between the carbonyl group of one amino acid and the amino group of another amino acid, stabilizing the helical structure. In a beta sheet, hydrogen bonds form between adjacent strands of the polypeptide chain, holding the sheet together.
Overall, the primary structure of a protein determines the sequence of amino acids, while the secondary structure refers to the local folding patterns that occur within the polypeptide chain. These structures are essential for the overall shape and function of a protein.
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Google Gemini AI
more than 3 weeks ago
Primary Structure
- Dehydration synthesis between amino acids by peptide bonds (-CO-NH-)
- Creates a polypeptide chain with an amino terminus (N-terminal) and a carboxy terminus (C-terminal)
- Sequence of amino acids is determined by DNA sequence
Secondary Structure
- Formation of regular patterns due to hydrogen bonding between amino acid backbone groups
- Two main types:
- Alpha (α) helix:
- Right-handed coil-like structure
- Formed by regular interactions between every fourth amino acid (i.e., i and i+4)
- Stabilized by hydrogen bonds between NH groups and CO groups
- Beta (β) sheet:
- Pleated sheet-like structure
- Formed by lateral association of two or more extended polypeptide chains
- Stabilized by hydrogen bonds between NH groups of one strand and CO groups of the adjacent strand, creating hydrogen bonds parallel to the axis of the sheet
- Dehydration synthesis between amino acids by peptide bonds (-CO-NH-)
- Creates a polypeptide chain with an amino terminus (N-terminal) and a carboxy terminus (C-terminal)
- Sequence of amino acids is determined by DNA sequence
Secondary Structure
- Formation of regular patterns due to hydrogen bonding between amino acid backbone groups
- Two main types:
- Alpha (α) helix:
- Right-handed coil-like structure
- Formed by regular interactions between every fourth amino acid (i.e., i and i+4)
- Stabilized by hydrogen bonds between NH groups and CO groups
- Beta (β) sheet:
- Pleated sheet-like structure
- Formed by lateral association of two or more extended polypeptide chains
- Stabilized by hydrogen bonds between NH groups of one strand and CO groups of the adjacent strand, creating hydrogen bonds parallel to the axis of the sheet
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