Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Are amino acids other than the usual 20 amino acids
found in proteins? If so, how are such amino acids incorporated
into proteins? Give an example of such an amino acid and a protein in which it occurs.
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Describe how the structure of immunoglobulins is related to their function.
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Describe how the structure of immunoglobulins is related to their function.
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- Are proteins with the same number of each different amino acid that form them necessarily identical proteins?arrow_forwardidentify both L-amino acidsarrow_forwardAttach an amino acid with the “-SH” functional group below. (not super long answers please) What is the name of the -SH functional group? What level of protein structure is determined by these amino acids? Explainarrow_forward
- Estimate the PI of the given amino acid? Assume that the amino acid contains a single carboxylic acid group on the side chain.arrow_forwardWhy do proteins hold their shape?arrow_forwardProteins that are synthesized by living organisms adopt abiologically active conformation. Yet when such moleculesare prepared in the laboratory, they usually fail to spontaneously adopt their active conformations. Can you suggestwhy?arrow_forward
- Draw one sample structure of the following types of amino acids: acidic amino acid, basic amino acid, non-polar amino acid polar, uncharged amino acid.arrow_forwardWhat are the building blocks of proteins? What type ofbond chemically connects these building blocks? What isthe importance of the R group?arrow_forwardWhen an inappropriate amino acid is substituted in place of another, as occurs in certain genetic disorders, the resulting protein is either poorly functional or non-functional. Since proteins contain hundreds if not thousands of amino acids, why should the change of a single amino acid be so critical?arrow_forward
- Describe three major functions of proteins in the human body with one example for each.arrow_forwardIt is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?arrow_forwardWhat are the "N" and "C" termini of proteins?arrow_forward
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