EBK ORGANIC CHEMISTRY
6th Edition
ISBN: 8220103151757
Author: LOUDON
Publisher: MAC HIGHER
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Question
Chapter 27, Problem 27.46AP
Interpretation Introduction
Interpretation:
The isoelectric point of lysozyme is to be identified.
Concept introduction:
The isoelectric point is the point where the
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Students have asked these similar questions
(b) Using alanine as an example, draw possible conformations of alanine in a peptide chain
and identify which conformer is favoured.
(c) Discuss how considering 'allylic strain' [see pages 33-39 of handout 1] can explain the
favoured conformation in part b above, and how this is relevant to the B-sheet
conformation in peptides/proteins.
h) 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?
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.
Chapter 27 Solutions
EBK 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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- 1. 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_forwardGive the amino acid sequence in the following tetrapeptide using both 3-letter and 1-letter abbreviations for the amino acids. (Capitalize amino zcid zbbreviations appropriately.) ball & stick + || labels Sequence (3-letter abbreviations) (Separate abbreviations with hyphens.) Sequence (1-letter abbreviations) (Do not separate abbreviations with hyphens.)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_forward
- c) Peptides and proteins have an amino terminus (N-terminus) and C-terminus. Do you think peptides and proteins can also react with ninhydrin and produce color? d) And will the peptides and proteins reaction with ninhydrin give you the actual amino acid concentration present in them? If yes, why? If no, why not? (= Make sure you provide explanation (rationale) to your answer)arrow_forward4: Draw structures from notations or notations from structures, for the following dipeptides. Look up in book for the structures of various amino acids and their names (and notations). (EOCQ 60) Hints for drawing a dipeptide from the specified amino acids. From the given symbols (Ser, Thr, etc), draw the structures for the amino acids in the specified order example, for Ser-Thr, draw Serine first and then Threonine). Then remove the OH from the first amin and one H (from the N atom) on the second amino acid. Then join the remaining fragments; that give the dipeptide formed. In these reactions, H2O is formed as a side product; but it is implied, and you have to show it in your answers. The following equation illustrates that. Here, R and R' are symbolic. In an actual question, you must the actual structures for the amino acids (Table 16.3 in the book). O H || | Н.N— CH— С-N-CH—С-ОН H,N-CH-C–OH + H,N-CH-Ċ–OH R' R. R' (H2O is a sid no need t Amino acid 2 dipeptide Amino acid 1 а. Cys-Ser…arrow_forwardAssume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a “random coil,” with many possible conformations. (a) What must be the sign of DS for the change: native à denatured? (b) How will the contribution of DS for native denatured affect the favorability of the process? What apparent requirement does this impose on DH if proteins are to be stable structures?arrow_forward
- (a) Redraw the tripeptide in zwitterionic form (b) Explain how ESI-MS can be used to determine which amino acid is in the middle of the sequence.arrow_forwardThe anticlotting property of heparin is partly the result of the negative charges it carries. ( Q.) Identify the functional groups that provide the negative charges.arrow_forwardNet 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)…arrow_forward
- Identify monomeric and multimeric (di-,tri-meric, for example) saccharides from this group. If you come across multimeric polypeptides, state the mono- mers that form these multimers. State the nature of the bond that links two units together in each case. (a) Maltose (b) Trehalose (c) Lactose (d) Sucrose (e) Cellobiose (f) Agarosearrow_forwardA. Amino Acids with Electrically Charged Side Chains Negative Pesitive Aspartie Acid Glutamie Acid (Asp D Lysine Histidine Arginine (Argl ® (Glul O (His H HO Ho HO -NH, -NH, NH, NH, -NH, NH NH H,N- ONH, ONH, C. Special Cases B. Amino Acids with Polar Uncharged Side Chains Proline Asparagine (Aan N Cysteine (Cya) © Glycine (Gly O Threonine Glutamine (Pra) P Serine (Ser 9 Но Họ Ho Ho Ho Но NH, NH, NH NH, NH, NH, -NH, но- SH он NH, NH, D. Amino Acids with Hydrophobic Side Chains Leucine (Leu O Phenylalanine (Phe e Tryptophan (Tp W Tyrosine Methionine Valine Isoleucine Alanine (Ala A IMe M Ho Ho Ho Ho HO NH, -NH, Но -NH, HO NH, NH, NH, NH, NH, NH он If the chromatogram was developed from reverse phase conditions, which of the following amino acids is expected to elute first? serine phenylalanine tryptophan O tyrosinearrow_forwardAnswer the following questions on the basis of the free energies of formation at 25°C shown in the table at the top of the next page: (a) Does the peptide bond between alanine and glycine form spontaneously under standard conditions?arrow_forward
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