2. Compare and contrast the biological roles of the following amino acids the following pairs of amino acids. Once you have documented these role state which member of the pair is most important and why (1-2 sentences) Pair #1 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Aspartic acid Glutamic acid Important in which pathways Pair #2 Arginine Histidine Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Pair #3 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Important in which pathways Tyrosine Phenylalanine

2. Compare and contrast the biological roles of the following amino acids the following pairs of amino acids. Once you have documented these role state which member of the pair is most important and why (1-2 sentences) Pair #1 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Aspartic acid Glutamic acid Important in which pathways Pair #2 Arginine Histidine Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Pair #3 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Important in which pathways Tyrosine Phenylalanine

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Choose the correct letter. For the peptide LCYR, what is the amino acid residue in the amino terminusa. Arginineb. Lysinec. Cysteined. Tyrosine All the following aren't characteristics of a biochemical reaction, except for *a. unspecificb. high orderlinessc. slow pacingd . none of the choices
2. Chymotrypsin, trypsin, and elastase are members of a family of enzymes referred to as serine proteases. The enzyme papain (found in papaya) is also a protease but is a member of a family of enzymes referred to as cysteine proteases. The amino acid residues in the active site of papain critical for peptide bond hydrolysis are a protonated histidine and a deprotonated cysteine residue. The cysteine residue functions as the nucleophile similarly to the serine residue in serine proteases. (a) Using what you know about chymotrypsin's mechanism, draw a reaction mecha- nisn for the hydrolysis of a peptide bond by papain. Does the mechanism you have drawn employ acid-base catalysis, covalent catalysis, (b) or both? (c) The pKa values of the active site residues that control the pH profile of the activity of pa- pain are 4.2 and 8.2. The pH optimum for the reaction is 6.0. Through the many years of re- search carried out on cysteine proteases, it has been demonstrated that the pKa of 4.2…
4. Show exactly which peptide bonds you would expect trypsin to cleave if you set a digest with the sample below. H3N+Gly Y lle Yval YCys Giu Gin Ala (Ser Yal Pro Cys Asp Leu Arg (Lys Phe Tyr) Asn FCO0- Lys Thr Leu Y His Would you expect to form the same peptides in the trypsin digest if you pretreat this sample with reducing agent (for example DDT)? Explain
On 4. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N-CH-C-N-CH-C- CH₂ CH₂ CH₂ NH CINH NH₂ Accessibility: Investigate CH₂ -NH -CH-C-N- CH-OH CH3 -CH-C-N CH₂ CH₂ -N- OH CHIC-OH CH₂ OH
please help in under 30 mins
Read very carefully: Chymotrypsin cleaves peptides C TERMINUS to the aromatic amino acids. Trypsin cleaves peptides C TERMINUS to basic amino acids. Cyanogen bromide (CNBR) cleaves C-terminus to methionine residues. With this knowledge, reconstruct the following cleavage products and give the original peptide sequence. CNBR Chymotrypsin WITHHERISALLRIGHT ISTRYWITHM Trypsin EISAM YWITHMEISAMANINGCHEMI STR YWITHHER 1 The which convorted e Name.
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
pls answer the following question. -Which amino acids contain the following?a.sulfur/sulfhydryl group b. aromatic group c. imidazole ring d. guanidine group e. indole group -Classify the following proteins according to their biological function: casein, albumin gluten, and myoglobin. -Which levels of protein structure organization are lost during hydrolysis and denaturation? -What is the Beer-Lambert's Law? Why is it relevant to the quantitative analysis of proteins? -What are the other protein components of milk aside from casein?
26. Which statement is not correct about globular protein? Enzymes are exampleof globular protein The core is nonpolar The surface is polar Give support to tissues 27. Upstream processing is: * Preservation of the protein Expression of theprotein by cells Isolation of protein Purification ofprotein
Allosteric interactions refer to
Please explain in detail
1. In the mechanism of action of triose phosphate isomerase, Lys12 is an essential amino acid in the flexible phosphate gripper loop that undergoes a large conformational change to trap the substrate in the active site excluding water and holding the phosphate group in the correct geometry for isomerization rather than dephosphorylation. What would be the effect of the mutation of Lys12 to the unusual amino acid shown below? Explain. protein backbone