UNIT 1 - BIOCHEMISTRY

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111 Terms

1
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Ratio of C, H and O in a carbohydrate

1:2:1

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<p>What do alpha-glucose polymers form?</p>

What do alpha-glucose polymers form?

Starch

<p>Starch</p>
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<p>What do beta-glucose polymers form?</p>

What do beta-glucose polymers form?

Cellulose

<p>Cellulose</p>
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<p>Which carbon determines whether a molecule is glucose or galactose? </p>

Which carbon determines whether a molecule is glucose or galactose?

#4

<p>#4</p>
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<p>(T/F) In Galactose, the hydroxyl group is at the bottom of the 4th carbon</p>

(T/F) In Galactose, the hydroxyl group is at the bottom of the 4th carbon

False. The hydroxyl is located on top.

<p>False. The hydroxyl is located on top.</p>
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<p>In alpha-polymers, the OH group attached to C #1 will be…</p>

In alpha-polymers, the OH group attached to C #1 will be…

On the bottom

<p>On the bottom</p>
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<p>Draw a glycosidic linkage between 2 glucose molecules.</p>

Draw a glycosidic linkage between 2 glucose molecules.

knowt flashcard image
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<p>What links are Starch molecules composed of? </p>

What links are Starch molecules composed of?

alpha 1-4 links for the chain, alpha 1-6 links for branches

<p>alpha 1-4 links for the chain, alpha 1-6 links for branches</p>
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What links is glycogen composed of?

alpha 1-4 links, alpha 1-6 links where it branches.

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<p>What links are cellulose molecules composed of? </p>

What links are cellulose molecules composed of?

beta-1-4 glycosidic linkages

<p>beta-1-4 glycosidic linkages</p>
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<p>What is homeostasis?</p>

What is homeostasis?

The internal balance that a cell membrane helps maintain.

<p>The internal balance that a cell membrane helps maintain.</p>
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<p>Word for fluid inside a cell?</p>

Word for fluid inside a cell?

Intracellular

<p>Intracellular</p>
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<p>What does the Hydroxyl group in Cholesterol align with? </p>

What does the Hydroxyl group in Cholesterol align with?

Polar (Phosphate) side of phospholipids

<p>Polar (Phosphate) side of phospholipids</p>
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<p>What is a peripheral protein + its position on a cell membrane? </p>

What is a peripheral protein + its position on a cell membrane?

  • A protein that is loosely bound to the surface of a membrane.

    • Helps with transportation + communication

    • “Identity marker”

<ul><li><p>A protein that is loosely bound to the surface of a membrane.</p><ul><li><p>Helps with transportation + communication</p></li><li><p>“Identity marker” </p></li></ul></li></ul><p></p>
15
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<p>What is an Integral/transmembrane protein + its position in a cell membrane? </p>

What is an Integral/transmembrane protein + its position in a cell membrane?

  • A protein embedded in the cell membrane

  • Channels + pumps proteins through the cell membrane

<ul><li><p>A protein embedded in the cell membrane</p></li><li><p>Channels + pumps proteins through the cell membrane</p></li></ul><p></p>
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<p>Function of glycoproteins in a cell membrane?</p>

Function of glycoproteins in a cell membrane?

  • Act as a receptor, “recognizes” hormones to permit access to the cell

<ul><li><p>Act as a receptor, “recognizes” hormones to permit access to the cell </p></li></ul><p></p>
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<p>Function of glycolipids in a cell membrane? </p>

Function of glycolipids in a cell membrane?

  • Lipids with a carbohydrate attached

  • Provide energy

    • Marker for cell recognition

<ul><li><p>Lipids with a carbohydrate attached</p></li><li><p>Provide energy</p><ul><li><p>Marker for cell recognition </p></li></ul></li></ul><p></p>
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What is a concentration gradient?

Difference between concentration on inside and outside of membrane

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What is a passive mechanism?

Substance moves w/concentration gradient and does not require energy

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<p>What is diffusion and does it require an energy input? </p>

What is diffusion and does it require an energy input?

  • Natural movement of ions/molecules from an area of higher concentration to lower concentration

    • Does not require energy

<ul><li><p>Natural movement of ions/molecules from an area of higher concentration to lower concentration </p><ul><li><p>Does not require energy </p></li></ul></li></ul><p></p>
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<p>What is simple diffusion? </p>

What is simple diffusion?

Molecules move via diffusion directly through the lipid bilayer

<p>Molecules move via diffusion directly through the lipid bilayer</p>
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<p>What is facilitated diffusion? </p>

What is facilitated diffusion?

  • The transport of ions/molecules across a membrane through a carrier protein

    • Occurs ALONG THE CONCENTRATION GRADIENT

<ul><li><p>The transport of ions/molecules across a membrane through a carrier protein</p><ul><li><p>Occurs ALONG THE CONCENTRATION GRADIENT</p></li></ul></li></ul><p></p>
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<p>What is a channel protein? </p>

What is a channel protein?

An integral protein that remainss open all the time so substances can ‘flow through’

<p>An integral protein that remainss open all the time so substances can ‘flow through’</p>
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<p>What is a carrier protein? How does it transport specific molecules?</p>

What is a carrier protein? How does it transport specific molecules?

  • A protein that binds to specific molecules, then changes them before releasing into the other side.

    • E.g glucose transporters

<ul><li><p>A protein that binds to specific molecules, then changes them before releasing into the other side. </p><ul><li><p>E.g glucose transporters</p></li></ul></li></ul><p></p>
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<p>What is Osmosis? </p>

What is Osmosis?

The movement of water from an area of higher to lower concentration.

<p>The movement of water from an area of higher to lower concentration. </p>
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What is Osmotic Concentration?

The concentration of all solutes in a solution

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What is a hypertonic concentration?

A solution with a higher solute concentration that another

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What does it mean when two solutions are isotonic?

They have the same solute concentration.

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What is Osmotic Pressure?

  • the pressure of a solution against a semipermeable membrane to prevent water from flowing across the membrane

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When referring to cell membranes, the use of hypertonic/hypotonic refers to…

The concentration of solutes OUTSIDE the cell.

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<p>How do isotonic solutions affect osmosis in cells?</p>

How do isotonic solutions affect osmosis in cells?

There is no net movement of water, it flows in both directions

<p>There is no net movement of water, it flows in both directions </p>
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<p>How do hypotonic solutions affect osmosis in cells?</p>

How do hypotonic solutions affect osmosis in cells?

  • Net movement of water is into the cell.

<ul><li><p>Net movement of water is into the cell.</p></li></ul><p></p>
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<p>What happens when an animal cell bursts due to too much water? </p>

What happens when an animal cell bursts due to too much water?

It Lyses

<p>It Lyses</p>
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<p>How do hypertonic solutions affect osmosis in cells?</p>

How do hypertonic solutions affect osmosis in cells?

The net movement of water is out of the cell

<p>The net movement of water is out of the cell</p>
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<p>What is it called when the cell membrane pulls away from the cell wall (PLANT) </p>

What is it called when the cell membrane pulls away from the cell wall (PLANT)

Plasmolysis

<p>Plasmolysis </p>
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What is it called when only one type of substance is actively transported through a membrane?

Uniport

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<p>What is a proton pump?</p>

What is a proton pump?

uses energy from ATP to pump hydrogen ions across the membrane

<p>uses energy from ATP to pump hydrogen ions across the membrane</p>
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<p>What is created as a result of the transportation of H+ ions, and what effect does it have on the concentration gradient? </p>

What is created as a result of the transportation of H+ ions, and what effect does it have on the concentration gradient?

  • A large difference in charge is created due to the charge of H+

  • Builds up a concentration gradient

    • Creates an electrochemical gradient that stores potential energy

<ul><li><p>A large difference in charge is created due to the charge of H+</p></li><li><p>Builds up a concentration gradient </p><ul><li><p>Creates an electrochemical gradient that stores potential energy</p></li></ul></li></ul><p></p>
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What is cotransport?

When two substances are simultaneously transported across a membrane by one protein.

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What are the two types of Cotransport?

  • Symport - Both substances going in the same direction

  • Antiport - Two substances are being transported in opposite directions

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What is Membrane-assisted transport?

Transport method used to move material too large to cross the cell memnbrane through a channel/carrier protein (REQUIRES ENERGY)

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<p>What is Endocytosis? </p>

What is Endocytosis?

  • When a cell absorbs material by folding the cell membrane around it, then pinching off

<ul><li><p>When a cell absorbs material by folding the cell membrane around it, then pinching off </p></li></ul><p></p>
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<p>What is phagocytosis? </p>

What is phagocytosis?

Endocytosis involving solid particles

<p>Endocytosis involving solid particles</p>
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<p>What is pinocytosis? </p>

What is pinocytosis?

Endocytosis involving liquid particles

<p>Endocytosis involving liquid particles </p>
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<p>What is receptor-mediated endocytosis (RME)? </p>

What is receptor-mediated endocytosis (RME)?

  • Parts of the cell membrane are covered in receptor proteins

  • These proteins will only bind to specific molecules

<ul><li><p>Parts of the cell membrane are covered in receptor proteins</p></li><li><p>These proteins will only bind to specific molecules</p></li></ul><p></p>
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<p>What is Exocytosis? </p>

What is Exocytosis?

A vesicle fuses with the cell membrane to release its contents outside of the cell.

<p>A vesicle fuses with the cell membrane to release its contents outside of the cell. </p>
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<p>What is an Enzyme? </p>

What is an Enzyme?

a protein catalyst

  • It speeds up chemical reactions without being consumed in the process

<p>a protein catalyst </p><ul><li><p>It speeds up chemical reactions without being consumed in the process </p></li></ul><p></p>
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<p>What is a substrate? </p>

What is a substrate?

A reactant in a reaction involving an enzyme

<p> A reactant in a reaction involving an enzyme </p>
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<p>What is an active site? </p>

What is an active site?

The region on an enzyme that substrates bind to.

<p>The region on an enzyme that substrates bind to. </p>
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<p>Explain:</p><ul><li><p>Lock and Key Model</p></li><li><p>Induced Fit Model</p></li></ul><p></p>

Explain:

  • Lock and Key Model

  • Induced Fit Model

Lock and Key Model:

  • Active site matches substrate exactly

Induced Fit Model:

  • Active site sort of fits substrate

  • Once substrate binds, functional groups of various amino acids react and shift, allowing the enzyme to change its shape to better accommodate the substrate

<p>Lock and Key Model:</p><ul><li><p>Active site matches substrate exactly</p></li></ul><p>Induced Fit Model:</p><ul><li><p><span>Active site sort of fits substrate</span></p></li><li><p><span>Once substrate binds, functional groups of various amino acids react and shift, allowing the enzyme to change its shape to better accommodate the substrate</span></p></li></ul><p></p>
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How do enzymes speed up a reaction?

They lower the activation energy required to ‘kick start’ a chemical reaction.

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Term for destroying a protein/other macromolecule

Denaturing

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<p>If enzymes do not change the overall reaction, then what do they do? </p>

If enzymes do not change the overall reaction, then what do they do?

They speed up the reaction by lining up the reactant(s). This lines up their bonds to be broken (and new ones formed), and allows for more collisions and overall a greater number of products

<p><span>They speed up the reaction by lining up the reactant(s). This lines up their bonds to be broken (and new ones formed), and allows for more collisions and overall a greater number of products</span></p>
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<p>Explain:</p><ul><li><p>Competitive Inhibitor</p></li><li><p>Non-competitive Inhibitors </p></li></ul><p></p>

Explain:

  • Competitive Inhibitor

  • Non-competitive Inhibitors

Competitive Inhibitor:

  • Similar to the substrate, binds to active site and blocks normal substrate from binding.

Non-competitive Inhibitors:

  • Bind to the enzyme at an allosteric (NOT ACTIVE) site, causing a change in the shape of the active site and preventing substrate from binding.

<p>Competitive Inhibitor:</p><ul><li><p>Similar to the substrate, binds to active site and blocks normal substrate from binding. </p></li></ul><p></p><p>Non-competitive Inhibitors:</p><ul><li><p>Bind to the enzyme at an allosteric (NOT ACTIVE) site, causing a change in the shape of the active site and preventing substrate from binding. </p></li></ul><p></p>
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<p>What is an ALLOSTERIC site? </p>

What is an ALLOSTERIC site?

A site that is not the active site.

<p>A site that is not the active site. </p>
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What is an allosteric inhibitor?

An inhibitor that binds to an allosterically controlled enzyme, stabilizing it and making it so that the enzyme CANNOT function

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<p>What is feedback inhibition? </p>

What is feedback inhibition?

  • Product of an enzyme-substrate complex travels back to inhibit an earlier enzyme in the reaction, interrupting the ‘steps’

<ul><li><p>Product of an enzyme-substrate complex travels back to inhibit an earlier enzyme in the reaction, interrupting the ‘steps’ </p></li></ul><p></p>
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What is it called when an enzyme and a substrate react?

An enzyme-substrate complex

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Glucose molecule (C6H12O6)

knowt flashcard image
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What is an intermolecular force?

A force that occurs between molecules

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Types of Intramolecular Bonds (2)

  • Ionic

  • Covalent

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What is Adhesion?

Tendency of water molecules to stick to other molecules

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<p>What functional group is this? </p>

What functional group is this?

Hydroxyl

<p>Hydroxyl</p>
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Draw a Carboxyl functional group.

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<p>What functional group is this? </p>

What functional group is this?

Amino

<p>Amino</p>
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<p>What functional group is this? </p>

What functional group is this?

Sulfhydryl

<p>Sulfhydryl</p>
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<p>What functional group is this?</p>

What functional group is this?

Phosphate

<p>Phosphate</p>
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What is a monomer?

The subunit of a polymer.

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What is a polymer?

A macromolecule.

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Name Monomers For:

  • Carbohydrates

  • Lipids (Fats)

  • Proteins

  • Nucleic Acids

  • Monosaccharides

  • Fatty acid/Glycerol

  • Amino Acids

  • Nucleotides

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<p>What is dehydration synthesis? What products does it form? </p>

What is dehydration synthesis? What products does it form?

  • Reaction that forms macromolecules out of their monomer units.

  • H2O and a polymer (liked via. an O atom) are formed as a product.

<ul><li><p>Reaction that forms macromolecules out of their monomer units.<br></p></li><li><p>H2O and a polymer (liked via. an O atom) are formed as a product.</p></li></ul><p></p>
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<p>What is an Anabolic reaction? </p>

What is an Anabolic reaction?

A reaction that produces large molecules from smaller subunits

<p>A reaction that produces large molecules from smaller subunits</p>
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What is Hydrolysis? What are its reactants?

  • Reaction that breaks macromolecules into its subunits

  • Reactants are a macromolecule and H2O

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Draw Glycerol

  • Hint: C3H8O3, 3 Hydroxyl groups

knowt flashcard image
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<p>What is a fatty acid?</p>

What is a fatty acid?

Hydrocarbon chain with a Carboxyl group on one end

<p>Hydrocarbon chain with a Carboxyl group on one end </p>
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Draw a triglyceride.

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<p>What is an ester linkage? </p>

What is an ester linkage?

Dehydration synthesis between a glycerol and three fatty acids.

<p>Dehydration synthesis between a glycerol and three fatty acids.</p>
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What is a saturated fatty acid?

Fatty acid has the maximum amount of hydrogen atoms (There are no double bonds between Carbon atoms)

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What fats are solid at room temperature?

Saturated fats.

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Two other types of lipids:

  • W___________

  • S___________

  • Waxes

  • Sterols

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Why are unsaturated fats liquid at room temperature?

  • The double-bonds in the carbon chains cause the HC chains to bend away, forming less bonds

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What is an immunoglobulin?

A protein that protects against foreign microorganisms + cancerous cells

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Possible functions of a protein (4)

  • Enzyme

  • Immunoglobulin

  • Protein carrier

  • Structural

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What is a protein conformation?

The final shape of a protein

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<p>Parts of an Amino acid (3) </p>

Parts of an Amino acid (3)

  • Amino group

  • Side chain

  • Carboxyl (COOH) group

<ul><li><p>Amino group</p></li><li><p>Side chain</p></li><li><p>Carboxyl (COOH) group </p></li></ul><p></p>
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<p>What is an R group? </p>

What is an R group?

Determines properties of an amino acid

<p>Determines properties of an amino acid</p>
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<p>What is a peptide bond? How do they form? </p>

What is a peptide bond? How do they form?

  • Holds amino acids together

  • Formed by a D.S reaction between the Amino group of an acid and the carboxyl group of an adjacent amino acid (O—N)

<ul><li><p>Holds amino acids together</p></li><li><p>Formed by a D.S reaction between the Amino group of an acid and the carboxyl group of an adjacent amino acid (O—N)</p></li></ul><p></p>
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What is a globular protein?

Composed of 1 or more polypeptide chain that takes a round/spherical shape

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<p>What is a primary protein structure? </p>

What is a primary protein structure?

  • Chain of amino acids held together by peptide bonds

<ul><li><p>Chain of amino acids held together by peptide bonds </p></li></ul><p></p>
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<p>What is a secondary protein structure? </p><p>Explain:</p><ul><li><p>Alpha (Helix)</p></li><li><p>Beta (Pleated sheets) </p></li></ul><p></p>

What is a secondary protein structure?

Explain:

  • Alpha (Helix)

  • Beta (Pleated sheets)

  • Formed by hydrogen bonds between O of a carboxyl group and H atoms of an amino group

Alpha (Helix) - Tight coil produces by H-bonds all at the same distance

Beta (Pleated sheets) - H bonds gormed between parallel stretches of a polypeptide

<ul><li><p>Formed by hydrogen bonds between O of a carboxyl group and H atoms of an amino group </p></li></ul><p>Alpha (Helix) - Tight coil produces by H-bonds all at the same distance</p><p></p><p>Beta (Pleated sheets) - H bonds gormed between parallel stretches of a polypeptide</p><p></p>
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<p>What is tertiary protein structure? </p>

What is tertiary protein structure?

  • Polypeptide chain is folded additionally due to interactions between R-groups

<ul><li><p>Polypeptide chain is folded additionally due to interactions between R-groups </p></li></ul><p></p>
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<p>What is a Disulphide Bridge?</p>

What is a Disulphide Bridge?

The bond formed between 2 sulphurs of nearby cysteines

<p>The bond formed between 2 sulphurs of nearby cysteines</p>
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<p>What is a Proline Kink? </p>

What is a Proline Kink?

A special kink in a polypeptide chain that occurs due to the presence of proline

<p>A special kink in a polypeptide chain that occurs due to the presence of proline </p>
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<p>What is quaternary protein structure? </p>

What is quaternary protein structure?

When 2 or more polypeptide chains come together and form a functional protein.

<p>When 2 or more polypeptide chains come together and form a functional protein. </p>
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Draw alpha-glucose

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Draw beta-glucose

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Draw sucrose

  • a-Glucose + Fructose

<p></p>
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Draw lactose

  • b Glucose + b Galactose

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Draw maltose

  • a-glucose + a-glucose

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Draw alpha-galactose

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