Identifying specific interactions between residues in a proteinImagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R2 come close to each other.In the table below are four possibilities for what R, and R₂ might be. In each case, decide whether a specific interaction could form between theresidues. If a specific interaction could form, give the name of the interaction.AZR₁R₂specificinteraction?name of specificinteractionO yescysteinecysteine0О поO yesIsoleucineOasparagineO noO yeslysineglutamate0O noO yesalanineisoleucineOO noExplanationCheck3WERaltoptioncmdH568H5ILLC. All Rights Reserved. Terms of UsePrivacy Center AccessibVBNMдвcmdPaltoption

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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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Calculate the molecular weight of a small protein if 5.90 g sample of this protein is dissolved in H₂O to make 563 mL of solution which has an osmotic pressure of 14.2 torr at 25°C. a) 1.53 x 10³ g/mol b) 1.37 x 104 g/mol e) 5.81 x 105 g/mol f) 9.74 x 106 g/mol g) 3.37 x 102 g/mol c) 7.23 x 10³ g/mol d) 3.54 x 105 g/mol
I don’t understand how to do part b of question 5. The other picture is my work of part a. How would changing the enzyme concentration affect Km and Vmax. The answer given to us is Vo= 0.796mM/s. I just don’t understand how to get to that answer.
Which protein folding interaction(s) is/are most likely to occur on the outside of a protein pocket in water (choose all that apply). a. hydrogen bonding b. hydrophobic effects c. salt bridge
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Which amino acid has a net charge of +0.09 at pH 7? Show all calculations. Draw the structure of the amino acid that would predominate at this this pH. Circle all atoms that can be involved in making hydrogen bonds at pH 7
Examine the protein shown below. Identify the predominate attractive force responsible for the protein's tertiary structure at the location circled in red. CH,OH но FCH, H,C- CH,OH носн, Select one: O H- bonding О Covalent O Dispersion O Dipole-dipole O lonic
Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other. In the table below are four possibilities for what R₁ and R2 might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ specific interaction? name of specific interaction x yes alanine valine O no isoleucine asparagine ○ yes O no yes lysine glutamate ☐ O no yes threonine asparagine O no
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Draw an a amino acid with an isopropyl (-CH(CH3)2) Continue side chain. Click and drag to start drawing a structure. C с с X 3 官 cx Ć
reaction LU Lake Piu Figure 1 (at right): Tertiary structure of the digestive enzyme trypsin from Streptomyces griseus. The substrate binds 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 which class (hydrophobic, polar, charged) does each belong? (You should be able to do this without looking at a table). O о TO-C-CH2-CH-C-O NH3 Charged hydrophobic CH3CH-C-O¯ NH3 O Charmed HO-CH2-CH-C-O H3N CH2CH2CH2CH2CH-C-O- Polar NH3 8. 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 the active site of an enzyme in order to interact with aspartate. Work with your team to explain.
The protein collagen has an isoelectric point of pl = 6.60. This is the pH at which the number of positive charges on the protein surface equals the number of negative charges on the protein surface. At which of the following solution pH values will collagen be in solution and at which will it tend to aggregate? pH = 12.89 pH = 4.07 PH = 6.50 Clear All The protein will be in solution. The protein will tend to aggregate.

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