Week 3- Protein Folding and Structure.pdf
3)(3 points) Why are a-helix and -sheets favored in protein structures.docx
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3)(3 points) Why are a-helix and ß-sheets favored in protein structures? 4) (6 points) Differentiate between primary, secondary and tertiary structure of proein Solution (3) Why alpha-helix and beta-sheets are favoured in protein structures: Proteins are synthesized from twenty amino acids, especially primary protein structures are a linear sequence of amino acids. In some cases, these polypeptide chain is folded through hydrogen bonding between amine nitrogen of one of the amino acid with C=O of another amino acids. This folding or coiling is called as alpha helix secondary protein structure. In other cases, proteins are not formed throgh coiling but stabilizes through hydrogen bonding between beta-sheets. In short, the hydrogen bonding plays crucial role in stabilizing proteins in secondary structures. Additionally, proteins generally seek to assume the conformation that is most thermodynamically stable. (4) Differentiate primary, secondary and tertiary structures of proteins: Primary Protein Structure: A linear and unique sequence of amino acids in a polypeptide chains. These amino acid are held by covalent bonds (like peptide bonds). Each polypeptide chain has a N-terminus and a C-terminus. This depends on the amino acid at the end of the polypeptide chain on either side. Secondary Protein Structure: The hydrogen bond is formed between the main-chain peptide groups results in the formation of secondary protein stucture. Here hydrogen bonding is formed between amines nitrogen and the carbonyl oxygens in different mino acids. There are two different types of Secondary Protein Structure, viz. alpha-helix and beta-sheets. In case of alpha helix, stucture looks loke a coil due to hyderogen bonding in main-chain peptides. On the other hand, hydrogen bonding is present between two strands of polypeptide chain. Tertiary Protein Structure: There are the special arrangements of secondary structure proteins. The alpha helix of beta sheets are further folded to form a tetiary preotein structure. This teriary structures is the complete 3-D structure of proteins. Thetetiary preotein structure is held together by noncovalent bonds such as hydrogen bonding and van der Waals forces. .
3)(3 points) Why are a-helix and -sheets favored in protein structures.docx
- 3)(3 points) Why are a-helix and ß-sheets favored in protein structures? 4) (6 points) Differentiate between primary, secondary and tertiary structure of proein Solution (3) Why alpha-helix and beta-sheets are favoured in protein structures: Proteins are synthesized from twenty amino acids, especially primary protein structures are a linear sequence of amino acids. In some cases, these polypeptide chain is folded through hydrogen bonding between amine nitrogen of one of the amino acid with C=O of another amino acids. This folding or coiling is called as alpha helix secondary protein structure. In other cases, proteins are not formed throgh coiling but stabilizes through hydrogen bonding between beta- sheets. In short, the hydrogen bonding plays crucial role in stabilizing proteins in secondary structures. Additionally, proteins generally seek to assume the conformation that is most thermodynamically stable. (4) Differentiate primary, secondary and tertiary structures of proteins: Primary Protein Structure: A linear and unique sequence of amino acids in a polypeptide chains. These amino acid are held by covalent bonds (like peptide bonds). Each polypeptide chain has a N-terminus and a C-terminus. This depends on the amino acid at the end of the polypeptide chain on either side. Secondary Protein Structure: The hydrogen bond is formed between the main-chain peptide groups results in the formation of secondary protein stucture. Here hydrogen bonding is formed between amines nitrogen and the carbonyl oxygens in different mino acids. There are two different types of Secondary Protein Structure, viz. alpha-helix and beta-sheets. In case of alpha helix, stucture looks loke a coil due to hyderogen bonding in main-chain peptides. On the other hand, hydrogen bonding is present between two strands of polypeptide chain. Tertiary Protein Structure: There are the special arrangements of secondary structure proteins. The alpha helix of beta sheets are further folded to form a tetiary preotein structure. This teriary structures is the complete 3-D structure of proteins. Thetetiary preotein structure is held together by noncovalent bonds such as hydrogen bonding and van der Waals forces.