Concept explainers
(a)
Interpretation:
Structural formula of bradykinin is to be drawn.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
In protein the amide bond can link together with two amino acids to form a peptide bond.
Primary structure of protein is a sequence in which the amino acids linked by peptide bond in a protein.
Bradykinin is a 9-amino acid peptide chain. The Sequence is
(b)
Interpretation:
Reason for the kinked secondary structure of bradykinin is to be identified.
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
In protein the amide bond can link together with two amino acids to form a peptide bond.
Primary structure of protein is a sequence in which the amino acids linked by peptide bond in a protein.
Bradykinin is a 9-amino acid peptide chain. The Sequence is
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
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- Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.arrow_forwardThe amino acid valine has a nonpolar side chain, whereas serine has a polar side chain. Make a diagram of the two amino acids.(a) Why is the valine side chain nonpolar, yet the serine side chain is polar?(b) Which amino acid's side chains are hydrophilic and which are hydrophobic?arrow_forwardWhich of the following statements about aromatic amino acids is correct? (a) All are strongly hydrophilic. (b) Histidine's ring structure results in its being categorized as aromatic or basic, depending on pH. (c) On a molar basis, tryptophan absorbs more ultraviolet light than tyrosine. (d) The major contribution to the characteristic absorption of light at 280 nm by proteins is the phenylalanine R group. (e) The presence of a ring structure in its R group determines whether or not an amino acid is aromatic.arrow_forward
- Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forward(a) A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such a molecule. What kinds of interactions (iso logous or heterologous) would stabilize each? (b) Suppose a tetramer, like hemoglobin, consists of two each of two types of subunits, a and B. What is the highest symmetry now possible?arrow_forwardConsider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil con- formations will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forward
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