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Flashcards in this deck (55)
  • What type of bond is formed when there is a complete transfer of electrons?

    Ionic bond

    chemistry bonds
  • Which type of interaction occurs between charged species?

    Ionic interactions

    chemistry interactions
  • What is the relationship between Kw and pH?

    Kw = [H+][OH-], pH = -log[H+]

    chemistry acid-base
  • Identify the 20 common amino acids.

    • Alanine
    • Arginine
    • Asparagine
    • Aspartic acid
    • Cysteine
    • Glutamic acid
    • Glutamine
    • Glycine
    • Histidine
    • Isoleucine
    • Leucine
    • Lysine
    • Methionine
    • Phenylalanine
    • Proline
    • Serine
    • Threonine
    • Tryptophan
    • Tyrosine
    • Valine
    biology amino_acids
  • Which amino acids are considered basic?

    • Arginine
    • Lysine
    • Histidine
    biology amino_acids
  • What types of interactions stabilize protein structures?

    • Ionic interactions
    • Dipole-dipole
    • Van der Waals
    • Hydrophobic effect
    • Cystine bridges
    biology proteins
  • What are the 4 levels of protein structure?

    • Primary
    • Secondary
    • Tertiary
    • Quaternary
    biology proteins
  • Describe the nature of the peptide bond.

    Rigid and planar

    biology proteins
  • What motifs are common in secondary protein structure?

    • Alpha helix
    • Beta sheet
    • Random coil
    • Beta turns
    biology proteins
  • What determines the folding of a protein?

    Sequence determines structure

    biology proteins
  • How are proteins separated by size?

    Centrifugation and size exclusion chromatography

    biology techniques
  • What is a monoclonal antibody?

    An antibody made from identical immune cells that are clones of a unique parent cell.

    biology immunology
  • Identify the difference between monoclonal and polyclonal antibodies.

    Monoclonal antibodies are derived from a single clone; polyclonal antibodies are from multiple clones.

    biology immunology
  • What is the purpose of antibodies in detecting antigens?

    They bind specifically to antigens for detection in assays like western blots and ELISAs.

    biology immunology
  • What is the key structural difference between hemoglobin and myoglobin?

    Hemoglobin binds oxygen cooperatively, while myoglobin does not.

    biochemistry proteins
  • What role does the distal histidine play in hemoglobin?

    It allows binding of O2 to heme iron and reduces hemoglobin's affinity for CO.

    biochemistry proteins
  • What is the proximal histidine's function in hemoglobin?

    It coordinates with the heme iron.

    biochemistry proteins
  • What results from oxygen binding to the heme group?

    It reduces the size of the heme iron, causing conformational changes.

    biochemistry proteins
  • What factors affect the T-R transition in hemoglobin?

    • O2 binding
    • CO2 levels
    • BPG
    • pH effects
    biochemistry hemoglobin
  • What is the significance of mutations in hemoglobin?

    They can lead to diseases like sickle-cell disease.

    biochemistry disease
  • What do enzymes do?

    They accelerate reaction rates necessary for life.

    biochemistry enzymes
  • What is the relationship between Gibbs free energy and reaction spontaneity?

    Large negative Gibbs free energy indicates a spontaneous reaction.

    biochemistry thermodynamics
  • How do enzymes affect activation energy?

    They lower the activation energy required for reactions.

    biochemistry enzymes
  • What does Vmax represent in enzyme kinetics?

    The maximum rate when all enzyme active sites are occupied.

    biochemistry kinetics
  • What is the Michaelis-Menten equation used for?

    To describe the rate of enzyme-catalyzed reactions.

    biochemistry kinetics
  • Why is the Km value important?

    It reflects the substrate concentration at which the reaction rate is half of Vmax.

    biochemistry kinetics
  • What type of residues does chymotrypsin prefer?

    Big hydrophobic residues due to the S1 binding pocket.

    biochemistry enzymes
  • What characterizes the burst phase in chymotrypsin action?

    It is observed at the start of the reaction, indicating rapid substrate conversion.

    biochemistry enzymes
  • What is the anomeric carbon in carbohydrates?

    The anomeric carbon is the carbon atom that is bonded to two oxygens in a cyclic sugar ring and determines the alpha or beta form.

    carbohydrates biochemistry
  • Differentiate between reducing and non-reducing sugars.

    Reducing sugars can donate electrons, whereas non-reducing sugars cannot.

    carbohydrates sugars
  • What are the common polysaccharides?

    • Starch
    • Glycogen
    • Cellulose
    carbohydrates polysaccharides
  • What is the structure of triacylglycerol?

    Triacylglycerol consists of three fatty acids esterified to a glycerol backbone.

    lipids triacylglycerol
  • What are the essential fatty acids?

    • Linoleic Acid (Omega-6)
    • Alpha-Linolenic Acid (Omega-3)
    lipids fatty_acids
  • What role does LDL play?

    LDL (Low-Density Lipoprotein) transports cholesterol to tissues and can contribute to plaque buildup in arteries.

    cholesterol lipids
  • How do lipid bilayers form?

    Lipid bilayers form spontaneously due to hydrophobic interactions between fatty acid tails and hydrophilic interactions with water.

    membranes lipids
  • What are the components of signal transduction?

    Key components include secondary messengers like Ca++, cAMP, diacyl glycerol, and phosphatidic acid.

    cell_biology signal_transduction
  • Define a catabolic pathway.

    A catabolic pathway breaks down molecules to release energy.

    metabolism pathways
  • What is the universal energy currency?

    ATP is the universal energy currency due to its thermodynamic instability and high phosphoryl transfer potential.

    metabolism atp
  • What role do bile acids play?

    Aid in digestion and absorption of fats

    Transport oxygen in blood

    Regulate body temperature

    Stimulate muscle contraction

    lipids bile_acids
  • The main classes of lipids include: - fatty acids - glycerolipids - sterols

    lipids classes
  • Describe the Na/K ATPase pump function.

    The Na/K ATPase pump transports Na+ out and K+ into the cell, crucial for maintaining membrane potential and glucose transport.

    membranes transport
  • What are the high energy electron carriers mentioned?

    • NADH
    • FADH2
    • FMNH2
    • NADPH
    biochemistry energy_carriers
  • What is the role of CoA in metabolism?

    Carries acetyl/acyl groups.

    biochemistry coa
  • What does Thiamine pyrophosphate help convert?

    Acetaldehyde.

    biochemistry thiamine
  • What molecule does UDP-glucose refer to?

    Glucose.

    biochemistry udp-glucose
  • What is the function of Biotin in metabolism?

    Incorporates CO2 into organic compounds.

    biochemistry biotin
  • In glycolysis, the overall logic is generating compounds with a higher phosphoryl transfer potential than ATP.

    metabolism glycolysis
  • Glycolysis consists of two phases: preparatory, making two phosphorylated 3-carbon molecules, and payoff — generates high phosphoryl potential molecules for the synthesis of ATP.

    metabolism glycolysis
  • What is the first enzyme in glycolysis and its action?

    Hexokinase catalyzes phosphorylation.

    metabolism glycolysis hexokinase
  • What type of reaction does Phosphofructokinase 1 catalyze?

    Phosphorylation.

    metabolism glycolysis phosphofructokinase
  • Identify the reaction catalyzed by Aldolase in glycolysis.

    Cleavage.

    metabolism glycolysis aldolase
  • What reaction is catalyzed by Glyceraldehyde 3-Phosphate Dehydrogenase?

    Oxidation.

    metabolism glycolysis glyceraldehyde
  • What is the reaction type performed by Phosphoglycerate kinase?

    Phosphorylation to generate ATP.

    metabolism glycolysis phosphoglycerate_kinase
  • Describe the action of Phosphoglycerate mutase.

    Isomerization.

    metabolism glycolysis phosphoglycerate_mutase
  • What does Enolase catalyze?

    Dehydration.

    metabolism glycolysis enolase
Study Notes

Core Concepts of Biochemistry

This document summarizes key topics for BCH 400, focusing on molecular interactions, amino acids, protein structure, and metabolism.

Review Quiz 1

Key Bond Types

  • Electronegativity: Understand ionic, polar covalent, and non-polar covalent bonds.

Non-Covalent Interactions

  • Ionic: Between charged species.
  • Dipole-Dipole: Polar interactions.
  • Van der Waals: Weak attractions.
  • Hydrophobic Effect: Non-polar interactions in water.

Properties of Water

  • Polarity: Affects hydrogen bonding.
  • Kw and pH Relationship: Important for acid-base chemistry.
  • Acids and Bases: Distinguish strong vs. weak.

Titration

  • Understand the titration of weak acids with strong bases and the Henderson-Hasselbalch equation.

Amino Acids

Common Amino Acids

  • Recognize 20 common amino acids by their properties.
  • Classify into acidic, basic, polar, and non-polar groups.
  • Memorize three-letter codes.

Protein Structure

Stabilizing Interactions

  • Interactions: Ionic, dipole-dipole, Van der Waals, hydrophobic effects, and disulfide bonds (cystine bridges).
  • Peptide Bond: Rigid and planar.
  • Secondary Structure: Main motifs include alpha helices and beta sheets.
  • Collagen Triple Helix: Unique structure with specific properties.

Protein Techniques

Protein Separation Techniques

  • Centrifugation: Uses size for separation.
  • Salting Out: Solubility-based technique.
  • Ion Exchange: Separated by charge; affected by pH.
  • Affinity Chromatography: Utilizes specific protein-ligand interactions.

Review Quiz 2: Antibodies

Antibody Production

  • B Cell Gene Rearrangement: Process of antibody formation.
  • Monoclonal vs. Polyclonal: Differences in origin and application.
  • Antigen Detection: Techniques like Western blots and ELISAs.

Hemoglobin and Myoglobin

Cooperative Binding

  • Hemoglobin: Exhibits cooperative binding to O2 via heme groups.
  • Binding Factors: Includes CO2, BPG, and pH. Sketch the binding curves.

Sickle-Cell Disease

  • Understand the molecular basis and mutations in hemoglobin affecting disease.

Enzyme Action

Enzyme Functionality

  • Specific Catalysts: Enzymes speed up reactions without altering equilibrium.
  • Cofactors: Essential for activity, often derived from vitamins.

Gibbs Free Energy

  • Determines spontaneity and relates to reaction rates via activation energy.

Enzyme Kinetics

Michaelis-Menten Kinetics

  • Km: Substrate concentration at half Vmax.
  • Vmax: Maximum reaction rate.
  • Lineweaver-Burk Plot: Linear representation of Michaelis-Menten equation.

Chymotrypsin

Function of Chymotrypsin

  • Amino Acid Roles: Important side chains in the catalytic mechanism.
  • Burst Phase: Initial rapid increase in reaction rate.

Carbohydrates

Basic Carbohydrate Structures

  • Recognize anomeric carbons, acetal/ketal moieties, and differentiate alpha/beta anomers.
  • Know reducing vs. non-reducing sugars and common polysaccharides.

Lipids

Major Lipid Classes

  • Understand fatty acid nomenclature (chain length, double bonds).
  • Identify essential fatty acids, eicosanoids, triacylglycerol, phospholipids, and sphingolipids.

Steroids and Membrane Function

Cholesterol and Lipoproteins

  • LDL and HDL Roles: Importance in circulation and health.
  • Bile Acids: Function and significance.

Membrane Structure

  • Formation of lipid bilayers and membrane fluidity regulation.

Metabolism

Pathways

  • Catabolic Pathways: Breakdown of molecules.
  • Anabolic Pathways: Synthesis of molecules.
  • ATP: Key energy currency, unstable yet kinetically stable.

Glycolysis Overview

Phases of Glycolysis

  • Preparatory Phase: Generation of phosphorylated intermediates.
  • Payoff Phase: Production of ATP. Understand key enzymes and their reactions.