Biochemistry and Organic Chemistry Overview
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Questions and Answers

What is the primary focus of biochemistry?

  • The creation of new chemical compounds.
  • The study of carbon-based compounds.
  • The examination of chemical processes in living organisms. (correct)
  • The analysis of all chemical elements.

Which of the following is NOT one of the four main groups of organic compounds found at the core of cellular structures and reactions?

  • Nucleic acids
  • Minerals (correct)
  • Carbohydrates
  • Lipids

What is a key characteristic of monosaccharides in solution?

  • They are typically non-polar and hydrophobic.
  • They contain only carbon and hydrogen atoms.
  • They are primarily insoluble in water.
  • They are polar, hydrophilic, and soluble in water. (correct)

Besides energy, what other primary function do carbohydrates serve?

<p>To provide structural support and aid in cell recognition. (A)</p> Signup and view all the answers

Which of these is an isomer of glucose?

<p>Fructose (C)</p> Signup and view all the answers

Which transport mechanism directly utilizes ATP as its energy source?

<p>Primary active transport (C)</p> Signup and view all the answers

What type of reaction joins monosaccharides to form disaccharides?

<p>Dehydration synthesis (A)</p> Signup and view all the answers

What is the driving force behind the movement of substances in simple diffusion?

<p>Concentration gradient (C)</p> Signup and view all the answers

Which disaccharide is composed of glucose and fructose?

<p>Sucrose (C)</p> Signup and view all the answers

Which of the following transport mechanisms involves the use of a vesicle to move large macromolecules?

<p>Bulk transport (D)</p> Signup and view all the answers

What type of linkage connects monosaccharides in complex carbohydrates?

<p>Glycosidic linkage (C)</p> Signup and view all the answers

What is the difference between symport and antiport in secondary active transport?

<p>Symport moves molecules in the same direction as the driving ion; antiport moves them in the opposite direction. (B)</p> Signup and view all the answers

Which polysaccharide is the primary energy storage molecule in plants?

<p>Amylose (A)</p> Signup and view all the answers

Which transport mechanism relies on integral proteins and a concentration gradient to move molecules across the cell membrane?

<p>Facilitated diffusion (A)</p> Signup and view all the answers

If a cell is placed in a hypertonic environment, how will water move across the cell membrane?

<p>Water will move out of the cell via osmosis (A)</p> Signup and view all the answers

What is the primary function of cellulose?

<p>Structural support in plant cell walls (A)</p> Signup and view all the answers

Which of the following is a key characteristic of lipids?

<p>They are primarily used as structural components of cell membranes and hormones. (C)</p> Signup and view all the answers

Which of these substances is transported by simple diffusion?

<p>Oxygen (A)</p> Signup and view all the answers

What is the basic structural unit of proteins?

<p>Amino acids (B)</p> Signup and view all the answers

What is the role of channel proteins in facilitated diffusion?

<p>To form a water-filled pore across the bilayer through which specific solutes can diffuse (B)</p> Signup and view all the answers

Which level of protein structure is determined by the sequence of amino acids?

<p>Primary structure (A)</p> Signup and view all the answers

What is a key factor that does NOT affect the fluidity of a cell membrane?

<p>The concentration gradient of ions across the membrane (D)</p> Signup and view all the answers

Which of the following processes is an example of bulk transport moving substances into the cell?

<p>Endocytosis (C)</p> Signup and view all the answers

What type of bonding primarily stabilizes the secondary structure of a protein?

<p>Hydrogen bonding (D)</p> Signup and view all the answers

What is the impact of changes in temperature or pH on a protein?

<p>They may cause denaturation of a protein. (B)</p> Signup and view all the answers

What is the process by which a protein loses its functional 3D shape called?

<p>Denaturation (C)</p> Signup and view all the answers

Which of the following is a common function of proteins?

<p>Catalyzing chemical reactions (B)</p> Signup and view all the answers

Which level of protein structure involves interactions between R groups of amino acids?

<p>Tertiary structure (D)</p> Signup and view all the answers

What type of proteins comprise the main components of muscles?

<p>Actin and myosin (D)</p> Signup and view all the answers

What level of protein structure involves the arrangement of multiple polypeptide chains into a functional complex?

<p>Quaternary structure (C)</p> Signup and view all the answers

Which of the following best describes the role of enzymes in biological reactions?

<p>They speed up reactions without being altered themselves. (A)</p> Signup and view all the answers

What is the active site of an enzyme?

<p>A specific region on an enzyme where a substrate binds. (C)</p> Signup and view all the answers

In the induced-fit model of enzyme function, what occurs just prior to substrate binding?

<p>The enzyme changes its shape slightly. (D)</p> Signup and view all the answers

What is the primary function of a cofactor in enzyme catalysis?

<p>To assist the enzyme in its catalytic activity. (D)</p> Signup and view all the answers

Which of the following is NOT a factor that affects enzyme activity?

<p>Presence of light. (D)</p> Signup and view all the answers

What is the mechanism of competitive inhibition on enzyme activity?

<p>The inhibitor binds to the active site, blocking the substrate binding. (B)</p> Signup and view all the answers

How does non-competitive (allosteric) regulation affect enzyme activity?

<p>The regulator molecule binds to the allosteric site, either activating or inhibiting the enzyme. (A)</p> Signup and view all the answers

What type of molecule serves as the assembly instructions for all proteins?

<p>Nucleic acids (A)</p> Signup and view all the answers

Which of the following is a key structural difference between DNA and RNA?

<p>DNA is double-stranded, while RNA is single-stranded. (D)</p> Signup and view all the answers

Which of the following is NOT a function of nucleotides?

<p>Building blocks of proteins. (A)</p> Signup and view all the answers

According to the document, what primary role does cholesterol play in cell membranes?

<p>It acts as a temperature buffer, maintaining membrane stability. (D)</p> Signup and view all the answers

How does increasing temperature affect membrane fluidity?

<p>Increases fluidity because of decreased attractions between phospholipids (C)</p> Signup and view all the answers

Which type of fatty acid tail would result in the greatest membrane fluidity?

<p>Short, unsaturated fatty acid tails. (A)</p> Signup and view all the answers

Considering an artificial cell membrane that must remain fluid at very warm temperatures, what would be the most appropriate design choice?

<p>Increase the amount of cholesterol and long tails to provide fluidity. (B)</p> Signup and view all the answers

What does feedback inhibition on enzyme activity involves?

<p>An allosteric inhibitor, product off the pathway it regulates (B)</p> Signup and view all the answers

Flashcards

Biochemistry

The study of the chemical compounds, reactions, and processes that occur within living organisms.

Organic Chemistry

The branch of chemistry that deals with compounds containing carbon, particularly those found in living organisms.

Macromolecule

Very large molecules, often formed by the joining of many smaller subunits.

Monosaccharide

Simple sugars that serve as the basic building blocks for more complex carbohydrates.

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Isomers

Sugars with the same chemical formula but different structural arrangements.

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Dehydration Synthesis

The reaction that joins two monosaccharides together by removing a water molecule.

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Glycosidic Linkage

A type of bond that links two monosaccharides together in a disaccharide.

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Disaccharide

A double sugar composed of two monosaccharides linked by a glycosidic linkage.

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Polysaccharide

A complex carbohydrate made up of many sugar units joined together by glycosidic linkages.

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Starch

A type of polysaccharide composed of many glucose units linked together by α-1,4 glycosidic linkages. Found in plants as an energy storage molecule.

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Glycogen

A type of polysaccharide composed of many glucose units linked together by α-1,4 and α-1,6 glycosidic linkages. Found in animals as an energy storage molecule.

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Cellulose

A type of polysaccharide composed of many glucose units linked together by β-1,4 glycosidic linkages. Found in plant cell walls and provides structural support.

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Lipid

A large and diverse group of biomolecules that are insoluble in water and have many important functions.

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Fatty Acid

A long chain of carbon atoms with a carboxyl group at one end. These chains can be saturated or unsaturated.

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Saturated Fatty Acid

A fatty acid where all carbon atoms are bonded to hydrogen.

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Unsaturated Fatty Acid

A fatty acid containing at least one double bond between carbon atoms.

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Triglyceride

A type of lipid composed of three fatty acids linked to a glycerol molecule. Used for energy storage.

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Phospholipid

A type of lipid composed of a glycerol molecule, two fatty acids, and a phosphate group. Important component of cell membranes.

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Steroid

A type of lipid with a characteristic four-ring structure. Examples include cholesterol and steroid hormones.

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Enzymes

Proteins that act as biological catalysts, speeding up chemical reactions without being consumed or altering the products.

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Substrate

The specific reactant that an enzyme binds to.

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Active Site

A small region on an enzyme where the substrate binds.

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Induced-Fit Model

A model describing how an enzyme changes shape to better accommodate its substrate.

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Co-factors

Non-protein groups that bind to enzymes and are essential for catalytic activity.

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Co-enzymes

Organic co-factors, often derived from vitamins.

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Competitive Inhibition

A type of enzyme regulation where an inhibitor binds to the active site, blocking substrate access.

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Non-competitive (Allosteric) Regulation

A type of enzyme regulation where a regulator molecule binds to an allosteric site, altering enzyme activity.

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Feed-back Inhibition

A type of allosteric inhibition where the product of a pathway inhibits its own production.

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Nucleic Acids

Large polymers composed of nucleotides, serving as the assembly instructions for all proteins.

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Nucleotide

The monomer unit of nucleic acids, containing a nitrogenous base, a sugar, and a phosphate group.

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DNA (Deoxyribonucleic acid)

The information-carrying nucleic acid found in all living organisms.

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RNA (Ribonucleic acid)

A nucleic acid involved in protein synthesis.

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ATP (Adenosine triphosphate)

The primary energy currency of cells, providing energy for most cellular functions.

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Simple diffusion

Movement of a substance across a cell membrane from a region of high concentration to a region of low concentration. Driven by the kinetic energy of the molecules.

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Osmosis

The diffusion of water across a semi-permeable membrane from a region of high water concentration to a region of low water concentration.

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Facilitated diffusion

Movement of a substance across a cell membrane from a region of high concentration to a region of low concentration with the aid of a channel or carrier protein.

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Active Transport

Movement of a substance across a cell membrane from a region of low concentration to a region of high concentration, against the concentration gradient. Requires energy from ATP.

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Primary Active Transport

Type of active transport that directly uses ATP as a source of energy to move substances across a membrane against their concentration gradient. Think of it like a pump using energy directly.

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Secondary Active Transport

Type of active transport that indirectly uses ATP by harnessing the electrochemical gradient created by primary active transport. Think of it like using the energy stored in a water reservoir.

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Endocytosis

Type of active transport where large molecules are transported into the cell by the formation of vesicles.

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Exocytosis

Type of active transport where large molecules are transported out of the cell by the fusion of vesicles with the plasma membrane.

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Selective permeability

The ability of a membrane to allow some substances to pass through while blocking others.

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Concentration Gradient

Differences in the concentrations of molecules across a membrane.

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Study Notes

Biochemistry

  • Biochemistry is the study of chemical compounds, reactions, and processes in living organisms.

Organic Chemistry

  • Organic chemistry is the study of carbon-containing compounds.
  • All organic compounds in living organisms are primarily composed of carbon, hydrogen, and oxygen atoms.

The Biochemical Basis of Life

  • Millions of complex chemical reactions occur in the body every second.
  • Cells consist of thousands of diverse chemical compounds organized into various structures.
  • Four main types of organic compounds form the basis of cellular structures and reactions: carbohydrates, fats (lipids), proteins, and nucleic acids.
  • These compounds are either synthesized by cells or derived from consumed foods.

Carbohydrates

Functions of Carbohydrates

  • Main energy source.
  • Raw material for building other molecules.
  • Structural support.
  • Cell identification/communication.

Monosaccharides (Simple Carbohydrates)

  • "Saccharide" means sugar.
  • Common monosaccharides have 3, 5, or 6 carbon atoms (triose, pentose, hexose).
  • Examples include fructose, glucose, and galactose (isomers).
  • Polar, hydrophilic, and water-soluble.
  • Can exist in linear or ring forms.

Disaccharides (Simple Carbohydrates)

  • Formed by joining monosaccharides via dehydration synthesis.
    • Formula: C12H22O11
  • Examples: maltose (glucose + glucose), sucrose (glucose + fructose), lactose (glucose + galactose).
  • Dehydration synthesis creates an ether linkage connecting the molecules.
  • Hydrolysis breaks the linkage using water.

Polysaccharides (Complex Carbohydrates)

  • Polymers of glucose.
  • Very polar and hydrophilic, but large size prevents full solubility.
  • Important for energy storage or structural support.
  • May be linear or branched (linked by different glycosidic bonds).
  • Energy storage:
    • Plants store α-glucose as starch (amylose - unbranched).
    • Animals store α-glucose as glycogen (highly branched).
  • Structural support:
    • Cellulose (unbranched), composed of β-glucose, forms plant cell walls.
    • Cellulose is indigestible for humans due to lacking the enzyme to recognize β linkages.

Lipids

Functions of Lipids

  • Energy source and storage.
  • Structural components of cell membranes.
  • Hormones (e.g., sex hormones, stress hormones).
  • Protection and insulation.
  • Vitamin source and absorption.

Saturated vs. Unsaturated Fatty Acids

  • Triglycerides, phospholipids, and steroids are types of lipids.
  • Steroids have four rings of carbon atoms.
  • Cholesterol is a precursor to many steroids.
    • Saturated have single bonds.
    • Unsaturated have double bonds creating kinks.

Proteins

  • Polymers of amino acids.
  • General structure: Carbon, hydrogen, oxygen, nitrogen, and sometimes sulfur.
  • 20 different amino acids (differing R groups).
  • 12 are non-essential, and 8 are essential.

Protein Structure

  • Primary Structure: Sequence of amino acids in a polypeptide chain.
  • Secondary Structure: Hydrogen bonding forms alpha-helices or beta-pleated sheets.
  • Tertiary Structure: 3D structure formed through interactions between R groups (hydrogen bonds, disulfide bridges, ionic bonds, hydrophobic interactions).
  • Quaternary Structure: Multiple polypeptide chains bonded together (some proteins). Prosthetic groups may be present.
  • Proteins can be fibrous (long and linear) or globular (compact).
  • Protein shape can be disrupted (denatured) by temperature or pH changes.

Protein Functions

  • Transport
  • Catalysis
  • Defense
  • Movement
  • Coordination
  • Storage
  • Binding

Enzymes

  • Control cellular activities.
  • Biological catalysts that increase reaction rates without being consumed.
  • Proteins with a unique 3D shape (active site) that determines their specific reaction.
  • Substrate binds to the active site (induced-fit model).
  • May require co-factors (often metals) or co-enzymes (organic molecules).

Enzyme Regulation

  • Competitive Inhibition: Inhibitor resembles substrate, competing for the active site.
  • Non-competitive (Allosteric) Regulation: Inhibitor binds to a different site, altering enzyme shape. Feed-back inhibition.
    • Often, the end product of a pathway is a non-competitive inhibitor of an earlier enzyme involved.
    • This slows down or stops the production of the product if there is already enough.

Nucleic Acids

  • Assembly instructions for proteins.
  • Types: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).
  • DNA stores hereditary information (eukaryotes, prokaryotes, many viruses).
  • RNA (mRNA, rRNA, tRNA) is involved in protein synthesis (hereditary molecule in some viruses).
  • Nucleic acids are polymers of nucleotides.
  • Nucleotides perform other functions (e.g., ATP, cAMP).

Plasma Membrane

  • Selectively permeable phospholipid bilayer.
  • Contains proteins (integral and peripheral) and carbohydrates.
  • Cholesterol affects fluidity.
    • High temp=high fluidity, adding cholesterol increases attraction, decreases fluidity.
    • Cold temp=low fluidity, cholesterol spaces phospholipids, increases fluidity.

Factors Affecting Membrane Fluidity

  • Temperature (higher temp=higher fluidity).
  • Tail length (shorter tails = higher fluidity).
  • Degree of saturation (unsaturated fatty acids = higher fluidity).
  • Cholesterol (stabilizes fluidity, buffering effect).

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Description

This quiz covers key concepts in biochemistry and organic chemistry, focusing on the biochemical basis of life and the role of carbohydrates. You'll explore the structure and function of organic compounds and their importance in living organisms. Test your understanding of how these compounds interact to sustain life.

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