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WGU C785 Final Exam With Correct Verified Answers 2026|2027.

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WGU C785 Final Exam With Correct Verified Answers 2026|2027. WGU C785 Final Exam With Correct Verified Answers 2026|2027. WGU C785 Final Exam With Correct Verified Answers 2026|2027. WGU C785 Final Exam With Correct Verified Answers 2026|2027. WGU C785 Final Exam With Correct Verified Answers 2026|2027.

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WGU C785
Course
WGU C785

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WGU C785 Final Exam With Correct Verified
Answers 2026|2027.

What Is The Basic Structure Of An Amino Acid? What Do They Look Like?

(ANS- Amino Group (NH2 Or NH3), Carboxyl Group (COO Or COOH), Alpha Carbon (C), And
Variable Group



How Do You Identify The 3 Different Types Of Side Chains: Non-Polar/Hydrophobic, Polar, And
Charged?

(ANS- Non-Polar/Hydrophobic - End With CH Or "Can't Have" Water. Polar - End With OH, SH, Or
NH. Charged - End With A Charge



What Kinds Of Bonds Do Each Of The 3 Different Types Of Side Chains Make? (ANS- Ionic,
Hydrophobic/Non-Polar, Charged



What Are The 4 Levels Of Protein Structure?

(ANS- Primary - Linear Structure, Secondary - Folded Into Helix Or Pleated Sheet Caused By
Hydrogen Bonding, Tertiary - 3D Structure Caused By Side Chain Interactions, Quaternary - 1+
Amino Acid Chains Combine = Multiple Subunits MUST Have 1+ Subunit



What Enviormental Change Breaks Each Type Of Bond?

(ANS- Hydrophobic - Temperature Change, Ionic - Salt Or Decreased Ph, Hydrogen -
Temperature, Change In Ph, Disulfide - Reducing Agents



What Type Of Amino Acid Side Chain Leads To Protein Aggregration? (ANS- Hydrophobic Bonds



How Do Environmental Changes Affect Protein Folding?

,(ANS- Extreme Temp Can Cause Hydrogen Bonds To Break Apart = Malformation Of Protein
Folding



How Do Mutations Affect Protein Structure? (ANS- Can Cause Structure To Change. Protein
Loses Form = Loses Function. May Form A Different Protein.



What Is An Electron?

(ANS- Negatively Charged Atom On Outer Ring For Bonding



What Is Energy:

(ANS- Power Derived Fro Chemical Interaction



What Are Covalent Bonds?

(ANS- Chemical Bond, Atoms Share 1+ Valence Electrons



What Is An Ionic Bond? (ANS- Bond Between Positive And Negative



What Is A Hydrogen Bond? (ANS- Weak Bond Between Positive And Negative



With An Amino?

(ANS- Piece Of Amino Acid, NH2 Or NH3



What Is A Carboyxl?

(ANS- Piece Of Amino Acid, COO Or COOH



What Is Hydrophobic?

(ANS- Doesn't Like Water, End With CH

,What Is Hydrophilic?

(ANS- Water Lovering, End With OH, NH, Or SH



What Is Disulfide Bond?

(ANS- Strongest Bond Between Reduction Agents, Formed Between SH's.



What Are Zwitterions?

(ANS- Amino With Positive And Negative Charges = Overall Charge Of Zero



What Is A Polypeptide

(ANS- Polymer Of Amino Acids




What Is Dehydration Synthesis?

(ANS- Process Of Forming Peptide Bonds



What Is Hydrolysis?

(ANS- Adding Water To Destroy Bonds



What Is An Alpha Helix?

(ANS- Twisted Secondary Structure, Formed By Hydrogen Bonds



What Is A Beta Sheet?

(ANS- Folded Second Structure Shape, Formed By Hydrogen Bonds



What Is Denaturation?

, (ANS- Loss Of Shape Duet O Interruption Of Chemical Bonds; Occurs Via Extreme Salt, Temp, Ph



What Is Aggregation?

(ANS- Clumping Of Inner Or Outer Cellular Proteins Caused By Misfolded Proteins Leading To
Diseases Such As Alzheimers, ALS, Parkinson's



How Do Enzymes Catalyze Reactions?

(ANS- Bind With Substrates To Decrease Activation Energy Required And Decrease Reaction Rate



How Do Enzymes Affect Reaction Rate And Activation Energy? (ANS- Decrease Activation Energy
And Decrease Reaction Rate



What Are The 4 Steps Of The Enzymatic Cycle?

(ANS- Enzyme Recognizes Substrate, Substrate Attracts The Enzyme; Enzyme- Substrate Complex
Is Formed; Enzyme-Product Complex Formed; Product Is Released, Enzyme Recycled



How Do Environmental Changes Affect Enzymes?

(ANS- High Heat, Ph Change, High Salt Concentration, And Reducing Agents Can Cause An
Enzyme To Lose Its Form/Lose Function



What Is A Competitive Inhibitor?

(ANS- Mimics Substrate And Takes Its Place On The Active Binding Site



What Is A Noncompetitive Inhibitor?

(ANS- Binds To Allosteric Site Causing Active Site To Change Shape = Preventing Substrate From
Binding With Enzyme

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