Concept explainers
Interpretation:
Example of a protein containing primarily beta-sheets and also identify the protein mentioned is globular or fibrous.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino functional group is
Secondary structure of protein is the repeating structural patterns (
Fibrous protein is a tough, water insoluble protein whose protein chains form fibers or sheets.
Globular protein is a water soluble protein whose chain is folded in a compact shape.
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- 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_forwardGlutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.arrow_forwardGive an example of a protein that has quaternary structure. How many polypeptide chains are present in this protein?arrow_forward
- A) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its examplearrow_forwardAmino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?arrow_forwardSuppose that the given peptide below is a segment in a globular protein's primary structure. Determine what would most likely be the type of secondary structure that it will form. Explain. T-L-S-A-R-I-D-Varrow_forward
- Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular proteins. Why?arrow_forwardConsider beta-sheet comprised of twelve amino acid residues (two strands of six residues each). How many hydrogen bonds should be formed between backbone atoms in this sheet?arrow_forwardWhich of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globularform.)(a) Leucine (b) Glutamate(c) Phenylalanine (d) Glutaminearrow_forward
- Fibrous proteins, globular proteins, and conjugated proteins are the three (3) primary kinds of proteins. Give a brief description of each kind and an example of each.arrow_forwardHemoglobin is a tetramer consisting of two a and two b chains. What level of protein structure is described in the above statement?arrow_forwardWhich of the following amino acids would you expect to find more often near the center of a folded globular protein? Which ones would you expect to find more often exposed to the outside? explain your answers. Ser, Ser-p (a Ser residue that is phosphorylated), Leu, Lys, Gln, His, Phe, Val, Ile, Met, Cys–S–S–Cys (two cysteines that are disulfide- bonded), and Glu. Where would you expect to find the most N-terminal amino acid and the most C-terminal amino acid?arrow_forward
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