Concept explainers
(a)
Interpretation:
Primary structure has to be explained based on structure, type of bond and molecular interaction.
Concept introduction:
Primary structure is the sequence of amino acid connected by peptide bond in a polypeptide chain.
(b)
Interpretation:
Secondary structure has to be explained based on structure, type of bond and molecular interaction.
Concept introduction:
Secondary structure is the arrangement of polypeptide chain, in a regular pattern of
(c)
Interpretation:
Tertiary structure has to be explained based on structure, type of bond and molecular interaction.
Concept introduction:
Tertiary structure is the folding of a single protein into a specific three dimensional shape, held by noncovalent interaction between the side chains.
(d)
Interpretation:
Quaternary structure has to be explained based on structure, type of bond and molecular interaction.
Concept introduction:
Quaternary structure is forms when two or more proteins chains assembles n a larger three-dimensional structure held together by noncovalent interaction.
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- Proteins are found to have two different types of secondary structures viz. a-helix and B-pleated sheet structures. a-helix structure of a protein is stabilised by: (i) Hydrogen bonds (ii) van der Waals forces (iii) Peptide bonds (iv) Dipole-dipole interactionsarrow_forwardHow do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could giverise to each interaction.(a) Hydrophobic interactions(b) Salt bridges (ionic interactions)arrow_forwardName two(2) interactions that maintain tertiary protein structure.arrow_forward
- Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be rightarrow_forwardis Tertiary protein structure come from secondary structure?How are they related?(do we need to build up a secondary structure before make it become tertiary?)arrow_forwardAt what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.arrow_forward
- All proteins have primary (1°), secondary (2°) and tertiary (3°) structure. In addition, some (but not all) proteins exhibit quaternary (4°) structure. Explain quaternary structure and why only some proteins exhibit that level of structure.arrow_forwardA mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)arrow_forwardFind a protein of your choice (rcsb.org), choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein?arrow_forward
- Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.arrow_forwardWhich of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryarrow_forwardWhich of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forward
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