reaction LU Lake PiuFigure 1 (at right): Tertiary structure of the digestiveenzyme trypsin from Streptomyces griseus. The substratebinds the active site, indicated with darker color.Critical Thinking Questions:6. Circle the active site of the enzyme in Figure 1.7. Circle the side chains in each amino acid below. To whichclass (hydrophobic, polar, charged) does each belong? (Youshould be able to do this without looking at a table).OоTO-C-CH2-CH-C-ONH3ChargedhydrophobicCH3CH-C-O¯NH3OCharmedHO-CH2-CH-C-O H3N CH2CH2CH2CH2CH-C-O-PolarNH38. Suppose that aspartate (the first amino acid shown in CTQ 7) is part of a substrate.Hypothesize which of the other three amino acid side chains might be present in theactive site of an enzyme in order to interact with aspartate. Work with your team toexplain.

Since aspartate is negatively charged due to its acidic side chain, it might interact with…

Answered: reaction LU Lake Piu Figure 1 (at…

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Look at the amino acids shown below. Their side chains are highlighted. Which amino acids have polar side chains? (choose all that do!)
4: 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…
Q1. Would an amino acid with the given side chain be most likely to be found in the hydrophobic or hydrophilic region of a protein? Circle one below. A. B. C. -CH₂-CH-CH3 I CH3 O -CH2-C-NH2 -CH-CH3 | ОН Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic region Circle one: Hydrophilic region // Hydrophobic region
7. For ech of the amino acids listed (a thrugh e) classify each as either polar, nonpolar, acidic, or basic. (see screenshot attached).
A4 Your enzyme is inhibited by one of the compounds depicted above. The inhibitor for your specific protein is indicated via the PDB protein code shown.On the basis of the enzyme’s structure, its substrate and mechanism of action, predict what type of enzyme inhibition ( i.e., competitive or non-competitive) may occur and justify why you think this is the case . (Up to 50 words) TYPE NOT WRITE.
In the box below draw the tetrahedral representation of the R enantiomer of the amino acid valine, CH3CH(CH3)CH(NH2)CO,H. • Use the wedge/hash bond tools to indicate stereochemistry where it exists. • Do not draw the amino acid in zwitterion form. opy aste ChemDoodle
Look at the amino acids shown below. Their side chains are highlighted. Which amino acids have polar side chains? (choose all that do!) H H,N-C-COOH H,N-C-COOH H,N-Ç-COOH H,N-C-COOH CH2 ÇH2 CH2 CH2 H. H. H-C-CH3 NH2 H H. H. H OH A В
An enzyme that is chemospecific (group specific) will. Select one: O a. specifically attack one end of a particular bond in preference over the other. O b. recognise only one functional group among several identical functional groups O c. distinguish between stereoisomers, recognising one pair of enantiomers or a single enantiomer.
Part II (25 pts) Instruction: You have learned about the enzymes. Give five examples of SPECIFIC enzymes and their function in the human body. Enzymes Function
In the box below draw the tetrahedral representation of the S enantiomer of the amino acid valine, CH3CH(CH3)CH(NH2)CO,H. • Use the wedge/hash bond tools to indicate stereochemistry where it exists. Do not draw the amino acid in zwitterion form. opy aste ChemDoodle
H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.
1. For an enzyme to catalyze a reaction, it must preferentially stabilize the transition state (TS) of the reaction. If an enzyme instead preferentially stabilizes the enzyme-substrate complex (ES), it fails to catalyze the reaction. Justify this observation using a reaction coordinate diagram (free energy (G) vs. reaction coordinate).

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