Protein Flashcards
Primary structure
specific linear sequence of amino acids
Secondary structure
- folds and coils at various locations of polypeptide due to hydrogen bonding in the polypeptide backbone.
Common structures: - β-pleated sheet
- α-helix
Tertiary structure
3D structure is determined by intermolecular reactions between R-groups in the polypeptide chain.
Quaternary structure
some proteins consist of 2 or more polypeptide chains aggregated into one functional macromolecule
E.g., Hemoglobin consists of 2 types of polypeptide chains (2 α, 2 β);
What is the basic structure of an amino acid? How many amino acids are there? How many are essential?
- Amino Acids contain:
1. a central carbon
2. an amino group (-NH2 or NH3+)
3. a carboxyl group (-COOH or COO-)
4. an H atom
5. a side chain (R) - There are 20 amino acids, 8 of which are essential (must obtain from diet) (**Note: some sources cite 9
essential amino acids)
What type of reaction occurs in the synthesis of peptides? What type of bond is formed?
During the synthesis of peptides (multiple amino acids) a dehydration synthesis reaction occurs bonding the amino acids creating a peptide joined by a peptide bond.
polypeptide
a peptide with more than 50 amino acids linked together
Define protein. How is a polypeptide different from a protein?
What is a Protein?
A protein is a large molecule made of amino acids, essential for many functions in the body, like enzymes, hormones, and structural support.
Difference Between Polypeptide and Protein:
- A polypeptide is a single chain of amino acids.
- A protein is one or more polypeptides folded into a functional shape.
Define denaturation. What factors cause a protein to denture? What are some practical examples?
Denaturation
Denaturation is when a protein loses its shape due to changes in pH, salt, or temperature, causing it to stop working.
Causes:
- pH changes
- Salt levels
- Heat
Example:
- Heat styling hair temporarily changes its structure.
Is denaturation irreversible, reversible or both? Explain.
Denaturation can be both reversible or irreversible, depending on the conditions and the protein involved.
- Reversible: If mild changes occur (e.g., slight temperature or pH shifts), proteins may regain their original shape and function when normal conditions are restored.
- Irreversible: If extreme changes happen (e.g., very high heat or strong acids), the protein structure is permanently altered, and it cannot return to its original form.
Example:
- Reversible: Some proteins may refold after a small temperature increase.
- Irreversible: Cooking an egg denatures its proteins permanently.