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Questions and Answers
What are unsaturated fatty acids?
What are unsaturated fatty acids?
What is the major function of fats?
What is the major function of fats?
Storing energy
Which statement describes phospholipids?
Which statement describes phospholipids?
What do anabolic reactions involve?
What do anabolic reactions involve?
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What are catabolic reactions characterized by?
What are catabolic reactions characterized by?
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What are nucleic acids made of?
What are nucleic acids made of?
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What is the primary function of nucleic acids?
What is the primary function of nucleic acids?
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Which of the following are types of nucleic acids?
Which of the following are types of nucleic acids?
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What is the main function of DNA?
What is the main function of DNA?
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What is the main function of RNA?
What is the main function of RNA?
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What are nucleotides composed of?
What are nucleotides composed of?
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A nucleoside contains a phosphate group.
A nucleoside contains a phosphate group.
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What is a phosphodiester bond?
What is a phosphodiester bond?
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Which of the following describe pyrimidines?
Which of the following describe pyrimidines?
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Which describe purines?
Which describe purines?
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RNA is usually double stranded.
RNA is usually double stranded.
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How is DNA structured?
How is DNA structured?
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What are the complementary base pairing rules in DNA?
What are the complementary base pairing rules in DNA?
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What happens during transcription?
What happens during transcription?
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What is translation?
What is translation?
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What is the central dogma of molecular biology?
What is the central dogma of molecular biology?
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What are proteins composed of?
What are proteins composed of?
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Which of the following best describes amino acids?
Which of the following best describes amino acids?
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What are peptides?
What are peptides?
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Polar amino acids have nonpolar side chains.
Polar amino acids have nonpolar side chains.
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What is the role of cysteine in proteins?
What is the role of cysteine in proteins?
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What is unique about glycine?
What is unique about glycine?
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What distinguishes proline from other amino acids?
What distinguishes proline from other amino acids?
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What are peptide bonds?
What are peptide bonds?
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What defines the primary structure of a protein?
What defines the primary structure of a protein?
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What is secondary structure in proteins?
What is secondary structure in proteins?
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What is tertiary structure in proteins?
What is tertiary structure in proteins?
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What characterizes quaternary structure of proteins?
What characterizes quaternary structure of proteins?
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What is a key feature of enzymes?
What is a key feature of enzymes?
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What are ribozymes?
What are ribozymes?
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What is the active site of an enzyme?
What is the active site of an enzyme?
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What is a substrate in enzymatic reactions?
What is a substrate in enzymatic reactions?
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What is an enzyme-substrate complex?
What is an enzyme-substrate complex?
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What is induced fit in enzyme activity?
What is induced fit in enzyme activity?
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What are cofactors?
What are cofactors?
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What are prosthetic groups?
What are prosthetic groups?
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What are coenzymes?
What are coenzymes?
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What is a metabolic pathway?
What is a metabolic pathway?
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What are enzyme inhibitors?
What are enzyme inhibitors?
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What describes irreversible inhibition?
What describes irreversible inhibition?
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What characterizes competitive inhibitors?
What characterizes competitive inhibitors?
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How do noncompetitive inhibitors work?
How do noncompetitive inhibitors work?
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What is allosteric regulation?
What is allosteric regulation?
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What are allosteric activators?
What are allosteric activators?
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What do allosteric inhibitors do?
What do allosteric inhibitors do?
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What role do protein kinases serve?
What role do protein kinases serve?
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What do protein phosphatases do?
What do protein phosphatases do?
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What is feedback inhibition?
What is feedback inhibition?
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What is the commitment step in a metabolic pathway?
What is the commitment step in a metabolic pathway?
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What are isozymes?
What are isozymes?
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What is the cell theory?
What is the cell theory?
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What is the plasma membrane?
What is the plasma membrane?
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What do both prokaryotic and eukaryotic cells have?
What do both prokaryotic and eukaryotic cells have?
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What does describe prokaryotic cells?
What does describe prokaryotic cells?
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What describes eukaryotic cells?
What describes eukaryotic cells?
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What are the three major parts of eukaryotic cells?
What are the three major parts of eukaryotic cells?
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What occurs in the nucleus?
What occurs in the nucleus?
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What are chromosomes made of?
What are chromosomes made of?
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What is the nuclear envelope?
What is the nuclear envelope?
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What is the function of the nucleolus?
What is the function of the nucleolus?
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What are ribosomes made of?
What are ribosomes made of?
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What is the cytoplasm?
What is the cytoplasm?
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What is the endomembrane system?
What is the endomembrane system?
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What does the rough ER do?
What does the rough ER do?
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What is the function of smooth ER?
What is the function of smooth ER?
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What is the Golgi apparatus's function?
What is the Golgi apparatus's function?
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What do lysosomes do?
What do lysosomes do?
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What is phagocytosis?
What is phagocytosis?
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What characterizes primary lysosomes?
What characterizes primary lysosomes?
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What defines a secondary lysosome?
What defines a secondary lysosome?
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What is autophagy?
What is autophagy?
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What organelles are not part of the endomembrane system?
What organelles are not part of the endomembrane system?
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What is the main function of mitochondria?
What is the main function of mitochondria?
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Which is a function of chloroplasts?
Which is a function of chloroplasts?
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What is chlorophyll?
What is chlorophyll?
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What are thylakoids?
What are thylakoids?
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What is stroma?
What is stroma?
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What similarities exist between mitochondria and chloroplasts?
What similarities exist between mitochondria and chloroplasts?
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What are peroxisomes?
What are peroxisomes?
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What are glyoxysomes?
What are glyoxysomes?
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What are vacuoles?
What are vacuoles?
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What makes up the cytoskeleton?
What makes up the cytoskeleton?
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What are microfilaments made of?
What are microfilaments made of?
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What is the role of intermediate filaments?
What is the role of intermediate filaments?
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What are microtubules?
What are microtubules?
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What are cilia?
What are cilia?
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What characterizes flagella?
What characterizes flagella?
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What do cell walls do in plants?
What do cell walls do in plants?
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What is the extracellular matrix?
What is the extracellular matrix?
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What are cell junctions?
What are cell junctions?
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What are plasmodesmata?
What are plasmodesmata?
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What are tight junctions?
What are tight junctions?
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What are desmosomes?
What are desmosomes?
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Study Notes
Unsaturated Fatty Acids
- Not saturated with hydrogen, characterized by double bonds or kinks in the carbon chain.
- Remain liquid at room temperature, important for cell membrane fluidity.
Fat Function
- Major role is energy storage within organisms.
Phospholipids
- Composed of a hydrophilic phosphate head and two hydrophobic fatty acid tails.
- Essential components of cell membranes, forming a bilayer that arranges with hydrophilic heads facing outward and hydrophobic tails inward.
Anabolic Reactions
- Involve the synthesis of complex molecules from simpler ones; require energy input.
- Considered endergonic reactions, where the free energy of products exceeds that of the reactants.
Catabolic Reactions
- Break down complex molecules into simpler ones, releasing energy.
- Classified as exergonic reactions, where the free energy of products is less than that of reactants.
Nucleic Acids
- Polymers made up of nucleotide monomers, crucial for storing and transmitting genetic information.
Function of Nucleic Acids
- Store, transmit, and utilize hereditary information through genes.
Major Nucleic Acid Types
- Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).
DNA Functions
- Stores genetic information, directs RNA synthesis, and controls protein synthesis.
RNA Functions
- Translates DNA sequences into polypeptides (proteins).
Nucleotide Structure
- Comprised of a 5-carbon sugar, a phosphate group, and a nitrogenous base.
Nucleoside Structure
- Consists of a pentose sugar and a nitrogenous base.
Phosphodiester Bond
- Links nucleotides through a condensation reaction; connects the hydroxyl group on the 3' carbon of one nucleotide to the phosphate group on the 5' carbon of another, forming the backbone of polynucleotides.
Pyrimidines and Purines
- Pyrimidines: single-ringed nucleotides (Cytosine, Thymine/Uracil in RNA).
- Purines: double-ringed nucleotides (Adenine, Guanine).
RNA Structure
- Typically single-stranded; can fold back on itself through hydrogen bonding.
DNA Structure
- Double helix structure, with hydrogen bonds forming between complementary bases (A-T and C-G pairing).
Base Pairing Rules
- DNA: C pairs with G, T pairs with A; RNA: C pairs with G, U pairs with A.
- C-G bonds are stronger than A-T bonds.
Transcription
- The process of transferring genetic information from DNA to messenger RNA (mRNA) within the nucleus.
Translation
- Involves the formation of a polypeptide (protein) where a ribosomal complex interprets mRNA.
Central Dogma
- Describes the flow of genetic information: DNA → RNA → Protein.
Proteins
- Polymers of amino acids, perform multiple roles including enzymatic activities, defense, regulation, and transport.
Amino Acids
- Composed of 20 common types; consist of an amino group, carboxyl group, and a variable side chain (R group).
Peptides
- Short chains of amino acids (20 or fewer), often act as signaling molecules or hormones.
Polar and Nonpolar Amino Acids
- Polar amino acids have hydrophilic side chains.
- Nonpolar amino acids are hydrophobic with nonpolar side chains.
Cysteine, Glycine, Proline
- Cysteine: Contains thiol groups, forms disulfide bridges, influencing protein folding.
- Glycine: Smallest amino acid, fits into tight spaces in proteins.
- Proline: Contains a ring structure, affecting protein geometry.
Peptide Bonds
- Covalent bonds formed between amino acids during dehydration synthesis; growth occurs from the amino terminus to the carboxyl terminus.
Protein Structures
- Primary: Sequence of amino acids.
- Secondary: Local folding patterns like α-helices and β-pleated sheets.
- Tertiary: Overall 3D structure formed by interactions between R-groups.
- Quaternary: Arrangement of multiple polypeptides into functional units.
Enzymes
- Specialized proteins that catalyze reactions without being consumed; commonly end in -ase.
Active Site and Substrate
- Active site: Area on enzyme where substrates bind specifically.
- Substrate: The reactant that undergoes a chemical change during enzymatic reaction.
Enzyme-Substrate Complex and Induced Fit
- Complex forms when substrates bind; induced fit model describes how binding alters shape to enhance catalysis.
Cofactors and Prosthetic Groups
- Cofactors: Non-protein components required for enzyme activity (may be inorganic).
- Prosthetic groups: Non-amino acid compounds permanently attached to enzymes.
Enzyme Regulation
- Competitive inhibitors: Compete with substrates for active site binding.
- Noncompetitive inhibitors: Bind elsewhere, altering enzyme shape and function.
- Allosteric regulation: Modulation of enzyme activity through non-active site binding.
Feedback Inhibition
- Pathway regulation where the end product inhibits the first enzyme to prevent overproduction.
Cell Theory
- All living organisms are made of cells, the cell is the basic unit of life, and all cells arise from pre-existing cells.
Plasma Membrane
- Acts as an outer barrier, selectively permeable; regulates entry/exit of substances.
Prokaryotic vs. Eukaryotic Cells
- Both contain DNA, ribosomes, cytosol, and a plasma membrane.
- Prokaryotic: No membrane-bound organelles, with a single circular chromosome.
- Eukaryotic: Membrane-bound organelles, multiple chromosomes within a nuclear envelope.
Eukaryotic Cell Parts
- Major components include the nucleus, cytoplasm, and plasma membrane.
Nucleus and Chromosomes
- Nucleus: Site of DNA replication and transcription, containing a nucleolus for rRNA synthesis.
- Chromosomes: Structures made from condensed chromatin, housing genetic information.
Ribosomes
- Composed of rRNA and proteins; essential for protein synthesis, either free in cytoplasm or attached to the rough ER.
Endomembrane System
- Composed of various organelles (e.g., ER, Golgi apparatus, lysosomes) involved in the synthesis, modification, and transport of proteins.
Endoplasmic Reticulum
- Rough ER: Studded with ribosomes for protein production and modification.
- Smooth ER: Synthesizes lipids and detoxifies harmful substances.
Golgi Apparatus
- Modifies ER products and dispatches them to destinations within or outside the cell.
Lysosomes
- Contain hydrolytic enzymes for breaking down macromolecules; involved in intracellular digestion.
Mitochondria and Chloroplasts
- Mitochondria: Site of ATP production through cellular respiration, double-membraned structure.
- Chloroplasts: Convert light energy into chemical energy through photosynthesis, also double-membraned.
Cytoskeleton
- Network of protein filaments providing structural support and facilitating organelle movement.
Cell Junctions
- Specialized structures that connect and bind adjacent cells; types include tight junctions, desmosomes, and plasmodesmata in plants for cytoplasmic flow.
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Description
Test your knowledge on the biochemistry of lipids, including unsaturated fatty acids, phospholipids, and the functions of fats. Additionally, explore anabolic and catabolic reactions essential for biochemical processes. This quiz will help solidify your understanding of molecular structures and energy dynamics.