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BIOC 7301 Biochemistry I Exam Review 2025-2026 Latest Questions with Correct and Verified, Exams of Nursing

BIOC 7301 Biochemistry I Exam Review 2025-2026 Latest Questions with Correct and Verified Answers Already A+ Graded-East Carolina University

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BIOC 7301 Biochemistry I Exam Review 2025-
2026 Latest Questions with Correct and
Verified Answers Already A+ Graded-East
Carolina University
What are the major elements in living organisms?
C, H, O, N
What are the minor elements in living organisms?
P, Na, K, Ca, Mg, S, Cl
What are trace elements in living organisms?
Fe, Zn, Cu
What are the 4 types of chemical bonds?
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Download BIOC 7301 Biochemistry I Exam Review 2025-2026 Latest Questions with Correct and Verified and more Exams Nursing in PDF only on Docsity!

BIOC 7301 Biochemistry I Exam Review 2025-

2026 Latest Questions with Correct and

Verified Answers Already A+ Graded-East

Carolina University

What are the major elements in living organisms? C, H, O, N What are the minor elements in living organisms? P, Na, K, Ca, Mg, S, Cl What are trace elements in living organisms? Fe, Zn, Cu What are the 4 types of chemical bonds?

  1. Covalent
  2. Ionic
  3. Hydrogen Bonds
  4. Weak Non-Polar Interactions
  • van der Waals
  • hydrophobic interactions What are the 5 unique properties of water?
  1. Cohesiveness/adhesiveness
  2. High heat capacity
  3. High heat of vaporization
  4. Expansion upon freezing
  5. Versatility as a solvent What is a Bronsted Acid? What is an Bronsted Base? Acid = proton donor Base = proton acceptor

Reduced - > Oxidized Alkane, Alcohol, Aldehyde, Ketone, Carboxylic Acid, Carbon Dioxide Catabolism releases energy by oxidizing carbon atoms by moving them to a higher oxidation state Anabolism uses energy to reduce carbon atoms by moving them to a lower oxidation state Reduced carbon contains energy that the cell can use. because it is fully reduced, it can be oxidized by using oxygen as the oxidizing agent and thus release the energy Oxidized carbon

has no energy that the cell can capture, only plants can extract energy and convert it to food source (photosynthesis) Stereoisomers D (R in organic chemistry) and L (S in organic chemistry) L is the preferred form in nature Non-Polar Amino Acids Alanine (Ala) Valine (Val) Leucine (Leu) IsoLuecine (Ile) Methionine (Met) Proline (Pro) Phenylalanine (Phe) Tryptophan (Trp)

What is the pKa of Lysine?

What is the pKa of Arginine?

What amino acid can form Disulfide bonds? Cysteine What is the charge of an amino acid at...

  1. pH 7
  2. pH 1
  3. pH 11
  4. 0 (Zwitter ion)
    • 1

What is an essential amino acid? It is an amino acid that cannot by synthesized by the organism and therefore is needed to be obtained through the diet. How does a peptide bond form? Through a condensation reaction which requires energy, enzymes, activated precursors + catalysis Planar Peptide Bonds Because of double bond character between C and O and C and N in a peptide, the alpha carbon (one with R group) can swivel. (Nth)peptide 20^n unique sequences

How to cleave (by reduce) a disulfide? Use Beta mercaptoethanol or dithiothreitol. Stabilize with iodoacetate How to cleave (by oxidize) a disulfide? Use HCOOOH What is Edman Degradatin? Sequential subtractive sequencing:

  1. Use Phenylisothiocyanate in alkai
  2. Trifluoracetic acid to selectively remove PTH-derivative
  3. Identify PTH-amino aicds by HPLC Automation - peptide attached to carboxyl terminal to insoluble bead. Cleavage Reagents
  1. Trypsin
  2. Chymotrypsin
  3. Staphylococcal protease
  4. Cyanogen bromide
  5. Lys or Arg
  6. Phe, Tyr or Trp
  7. Glu or Asp
  8. Met Cuts at C terminal Secondary/Tertiary/Quaternary Protein Structures are consequences of primary structure and its interactions with aqueous environment. most native protein structure is achieved by spontaneous folding into thermodynamically low energy form that does not require enzyme catalysis or external energy. sometimes aided by molecular chaperones which require ATP

True or False: Tertiary is a spontaneous event? True Salting out procedure

  1. Add salt to aqueous solution of proteins.
  2. Because salt and protein compete for water, protein molecules aggregate and precipitate.
  3. Protein redissolves if salt is removed. Salt of choice: ammonium sulfate (pure, soluble, gentle) Gel filtration chromotography Separates proteins by size. Smaller molecules enter beads and are slowed down. Large molecules flow around beads and exit faster.

Ion Exchange Chromatography Based on attraction between charged groups in protein and column medium. Selective absorption and elution accomplished by changing pH or salt concentration. Affinity Chromatography Based on selective binding of ligand by binding protein.

  1. Ligand linked to insoluble column medium.
  2. Pass proteins through column
  3. Only binding protein is absorbed
  4. Elute with high concentration of unbound ligand PAGE
  5. Form gel by polymerizing acrylamide with bis-acrylamide in buffer solution.
  6. Load protein sample
  7. Apply electrical voltage to separate proteins based on charge and size
  8. Detect with stain or x-ray X-ray crystallography

1 U = 1umole product/min Specific activity of an enzyme is ratio of enzyme activity to amount of protein (units/mg) which is (umole product/min/mg) Specific activity increases as enzyme is purified What is turnover number? It is the maximum number of molecules of substrate that an enzyme can convert to product per catalytic site per unit of time. kcat = Vmax/[E] What is a coenzyme? It is a low molecular weight organic compound which cooperates with an enzyme to facilitate reaction catalysis. can be a substrate or product

What are the two types of linkages in ATP? Phosphoanhydride linkages (2) and phosphoester linkage (1) Vitamin vs Coenzyme Many coenzymes have structures that are derived from vitamins which are nutritional requirements because organism is unable to synthesize it itself. (Niacin) NAD+ is involved in what type of reactions? NADP+? Catabolic, anabolic 3 parts of Flavin Adenine Dinucleotide Isoalloxazine, ribitol, riboflavin

What is the pH of a 0.01 M solution of HCl? 0.01 M HCl = 10^-2 M HCl = pH 2 ( dont use H-H equation) A buffer solution is prepared by mixing 10 mL 1M HA with 1 ml of 1 M NaA and diluting to a final volume of 100ml. What will be the pH of this buffer solution? The pK for HA is 4. (Use H-H equation) 10 ml 1M HA = 0.01 equivalents of HA When you have .01 equivalents (moles) of acid in a volume of 100ml it is the same as 0. equivalent/liter or .1M or 10^-1 M. 1ml of 1 M NaA = .001 equivalents of NaA When you have .001 moles of base in a volume of 100ml it is the same as. equivalents/liter or .01M or 10^- 2 pH = pK + log(base/acid) = 4 + log (.01 M/.1M) = 4 + log 1/ = 4- 1 = 3

** at this point you have 90% acid and 10% base and you are 1 pH unit below the pK. A buffer soltuion is prepared by mixing 10 ml 1M HA with 10 ml of 1M NaA and diluting to a final volume of 100ml. What will be the pH of this buffer solution? the pK for HA is 4. 10 ml 1M HA = 0.01 equivalents of HA When you have .01 equivalents (moles) of acid in a volume of 100ml it is the same as 0. equivalent/liter or .1M or 10^-1 M. 10 ml of 1M NaA = .01 equivalents of NaA When you have .01 moles of base in a volume of 100 ml it is the same as 0. equivalent/liter or .1M or 10^-1 M pH = pK + log (base/acid) = 4 + log (.1M/.1) = 4 + log 1/ = 4- 0 = 4 ** at this point you have 50% acid and 50% base and the pH equals the pK.