Organic Chemistry
6th Edition
ISBN: 9781936221349
Author: Marc Loudon, Jim Parise
Publisher: W. H. Freeman
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Question
Chapter 27, Problem 27.22P
Interpretation Introduction
(a)
Interpretation:
The exaplaination for the fact that amino acid
Concept introduction:
The amino acid is made of two
Interpretation Introduction
(b)
Interpretation:
The other pair of amino acid that is not distinguished on amino acid analysis in Peptide P is to be stated.
Concept introduction:
The amino acid is made of two functional groups an amine group
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indicate the RIGHT alternative:
(a) The Zwitterion form of an amino acid exists only at a point pH value.
(b) In a peptide bond there is free rotation at the C-N bond.
(c) In a polypeptide, the terminal carboxyl group may be present in its amide form.
(d) At a pH greater than pI, an amino acid tends to move towards the cathode in an electrophoresis.
(e) At any pH below pI, the predominant form of an amino acid is negatively charged.
Net charge and isoelectric point of an amino acid with an ionizable side group.Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(a) Identify the acidic amino acid(s) capable of having a negatively charged carboxyl side group.(b) Identify the basic amino acid(s) capable of having a positively charged amino side group.(c) For an amino acid with a side (R-) chain that can ionize to a negative charge, derive a general expression in terms of measured pH and known pKa values of α-carboxyla-amino (pKca), α-amino(pKaa),and side group (pKRa), respectively, for the net charge of an amino acid Consider the net charge and isoelectric point of an amino acid with ionizable side (R-) group.(d) For an amino acid with a side (R-) chain that can ionize to a positive charge, derive a general expression in terms of measured pH and known pKa values ofα-carboxyl (pKca), α-amino (pKaa), and side group (pKRa), respectively, for the net charge of the amino acid.(e)…
(b) Which of the following common amino acids has more than one amino group?
Chapter 27 Solutions
Organic Chemistry
Ch. 27 - Prob. 27.1PCh. 27 - Prob. 27.2PCh. 27 - Prob. 27.3PCh. 27 - Prob. 27.4PCh. 27 - Prob. 27.5PCh. 27 - Prob. 27.6PCh. 27 - Prob. 27.8PCh. 27 - Prob. 27.9PCh. 27 - Prob. 27.10PCh. 27 - Prob. 27.11P
Ch. 27 - Prob. 27.12PCh. 27 - Prob. 27.13PCh. 27 - Prob. 27.14PCh. 27 - Prob. 27.15PCh. 27 - Prob. 27.16PCh. 27 - Prob. 27.17PCh. 27 - Prob. 27.18PCh. 27 - Prob. 27.19PCh. 27 - Prob. 27.20PCh. 27 - Prob. 27.21PCh. 27 - Prob. 27.22PCh. 27 - Prob. 27.23PCh. 27 - Prob. 27.24PCh. 27 - Prob. 27.25PCh. 27 - Prob. 27.26PCh. 27 - Prob. 27.27PCh. 27 - Prob. 27.28PCh. 27 - Prob. 27.29PCh. 27 - Prob. 27.30PCh. 27 - Prob. 27.31PCh. 27 - Prob. 27.32PCh. 27 - Prob. 27.33PCh. 27 - Prob. 27.34PCh. 27 - Prob. 27.35PCh. 27 - Prob. 27.36PCh. 27 - Prob. 27.37PCh. 27 - Prob. 27.38PCh. 27 - Prob. 27.39PCh. 27 - Prob. 27.40PCh. 27 - Prob. 27.41PCh. 27 - Prob. 27.42PCh. 27 - Prob. 27.43APCh. 27 - Prob. 27.44APCh. 27 - Prob. 27.45APCh. 27 - Prob. 27.46APCh. 27 - Prob. 27.47APCh. 27 - Prob. 27.48APCh. 27 - Prob. 27.49APCh. 27 - Prob. 27.50APCh. 27 - Prob. 27.51APCh. 27 - Prob. 27.52APCh. 27 - Prob. 27.53APCh. 27 - Prob. 27.54APCh. 27 - Prob. 27.55APCh. 27 - Prob. 27.56APCh. 27 - Prob. 27.57APCh. 27 - Prob. 27.58APCh. 27 - Prob. 27.59APCh. 27 - Prob. 27.60APCh. 27 - Prob. 27.61APCh. 27 - Prob. 27.62APCh. 27 - Prob. 27.63APCh. 27 - Prob. 27.64APCh. 27 - Prob. 27.65APCh. 27 - Prob. 27.66APCh. 27 - Prob. 27.67APCh. 27 - Prob. 27.68APCh. 27 - Prob. 27.69APCh. 27 - Prob. 27.70APCh. 27 - Prob. 27.71APCh. 27 - Prob. 27.72APCh. 27 - Prob. 27.73APCh. 27 - Prob. 27.74APCh. 27 - Prob. 27.75APCh. 27 - Prob. 27.76APCh. 27 - Prob. 27.77APCh. 27 - Prob. 27.78APCh. 27 - Prob. 27.79APCh. 27 - Prob. 27.80APCh. 27 - Prob. 27.81APCh. 27 - Prob. 27.82APCh. 27 - Prob. 27.83AP
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- Draw three-dimensional representations of the following amino acids.(a) l-phenylalaninearrow_forwardExplain what is meant by the following :(i) peptide linkage(ii) pyranose structure of glucosearrow_forward1. It is observed that as temperature is increased, most protein molecules go from their defined, folded state into a random-coil, denatured state that exposes more hydrophobic surface area than is exposed in the folded state. (a) Given what you have learned so far about AH and AS, explain why this is reasonable. (b) Sometimes, however, proteins denature as temperature is decreased. How might this be explained?arrow_forward
- In relation to the spatial structure of the proteins select the INCORRECT alternative: (a) The quaternary structure of proteins consists of the association of two or more protein chains to form the complete protein. (b) The tertiary structure of proteins is mainly due to long-range interactions between amino acids that are far apart in the protein sequence but spatially close due to protein coiling. (c) Disulfide bridges are produced or broken as a result of oxidation-reduction processes. (d) The interactions between peptide chains in the secondary structure of proteins are basically due to Van der Waals forces. (e) The primary structure of proteins is basically due to the existence of covalent bonds between the different amino acids that constitute them.arrow_forwardDraw the tetrapeptide below out in full chemical structure by attaching the four amino acidsin order (this is an application of the characteristicorganic reaction Formation of an Amide. You can use any chemical notation orcombination of notations to draw your structure, but all bonds and atoms must be shown. Tyr-Cys-Met-Hisarrow_forwardThe use of salt bridges or hydrophobic interactions (or pockets) to stabilize interactions between more distant amino acids within a single polypeptide, is a demonstration of protein TERTIARY structure. True Falsearrow_forward
- Indicate whether each statement is true or false. (a) Thesequence of amino acids in a protein, from the amine endto the acid end, is called the primary structure of the protein.(b) Alpha helix and beta sheet structures are examplesof quaternary protein structure. (c) It is impossiblefor more than one protein to bind to another and make ahigher order structure.arrow_forwardh) Specify the absolute (R/S) configuration of the amino group in structure IV. (i) If the substituents in structures I, IV and V were identical (all OH or all NH2), which structure would result in a meso compound? (j) If each hydroxy group for structures I, II and VI were replaced with another amino group, which compound would be made optically inactive?arrow_forwardThe amino acid (S)-alanine has the physical characteristics listed under the structure. How does the melting point of a racemic mixture of (R)- and (S)-alanine compare to the melting point of (S)-alanine?arrow_forward
- (a) Which amino acid is present in higher amounts than glycine?(b) How many more molecules of that amino acid are presentthan the number of molecules in 1.0 mole of glycine?arrow_forward5. Arg and Lys Asp and Lys Pro and Glu Among these amino acid combinations listed above, only the combination of Asp and Lys have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain in your own words and by drawing (1) why Asp and Lys side chain interaction stabilizes the tertiary structure of a protein, and (2) why the pairs of Arg and Lys & Pro and Glu cannot provide the stability to the protein structure.arrow_forwardWhich of the common amino acids is not chiral? Sketch its structure and explain why it does not manifest chirality.arrow_forward
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