Biological Molecules Flashcards

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1
Q

What are the 3 types of Proteins and features

A

Globular:

  • Compact, soluble, spherical shaped.
  • Tertiary structure
  • hydrophillic on the outside, so soluble

Fibrous:

  • Long, insoluble
  • high presence of hydrophobic R groups in primary structure

Conjugated:

  • Are Globular proteins that contain a prosthetic group
  • E.g. Haemoglobin Fe 2+
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2
Q

What are the 3 polysacharides and features

A

Amylose/Amtlopectin

  • Alpha Glucose
  • Carbohydrate storage in plants
  • insoluble
  • long coiled chain
  • compact

Glycogen:

  • Alpha Glucose
  • Carbohydrate storage in Animals
  • Insoluble, compact due to branching

Cellulose

  • Beta Glucose
  • Structural support
  • Cross links
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3
Q

Structure of Alpha and beta glucose + polymer

A

Beta glucoss:

  • OH above
  • Bond by one turning upside down

Alpha Glucose:

  • OH below
  • O bonded to Ch2OH , making water
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4
Q

What are the 3 Disacharrides and how are they made

A

Maltose —> Glucose + Glucose
Lactose —-> Glucose + Galactose
Sucrose —-> Glucose + Fructose

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5
Q

What bond is formed when two monosacharrides join together

A

Glycosidic Bond via Oxygen

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6
Q

What are the properties of Water

A
  • 104.5 bonding angle
  • Polar slightly +ve and -ve charges
  • Relatively high boiling point compared to same size molecules
  • Cohesive - Molecules attracted to each other, moves as one mass
  • less dense when solid than liquid
  • Water coolant- Buffer temper changes
  • Medium- Chemical reactions/ transport dissolved compounds in and out cell
  • Surface tension supports small organisms
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7
Q

What are the 3 fibrous proteins and where are they found

A

Collagen- Found in skin, tendons, ligaments and nervous system

Keratin- Hair, skin, Nails

Elastin - Walls of blood vessels and alveoli of lungs

Provides resiliencr and elasticity to tissues and organs

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8
Q

3 Main proteins, structure and functions

A

Haemoglobin

  • Conjugated protein
  • Quaternanry structure
  • two alpha and beta sub units
  • Transporting oxgyen around the body

Enzyme

  • Made up of amino acids linked together with peptide bonds
  • Biological catalyst

Insulin

  • Globular protein
  • Soluble, Hormone
  • have precise shapes as need to fit into receptors on cell surface membrane to have their effect
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9
Q

What is the test for Reducing sugars

A

1) Sample in test tube/ boiling tube
2) Equal volume of Benedicts Reagent
3) Heat—> water bath 5 minutes
4) Reducing sugars react with Cu 2+ ions

BLUE To Brick RED

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10
Q

What is the main non reducing sugar and how is it tested

A

Sucrose

  • After negative benedicts test, boil with dilute HCL
  • Conduct benedicts test 2nd time.
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11
Q

What is the Emulsions test for Lipids

A

Mix sample with Ethanol
Mix with water and shake
Emulsion forms
Turns white/ cloudy

(Stain sudan 111)

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12
Q

What is the test for starch (Hint: Iodine)

A

Few drops of iodine dissolved in potassium iodide mixed with sample

Solution turns yellow/ brown to black/ purple (if starch is present)

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13
Q

What is the Formula of RF

A

Distance moved by amino acid
—-‐———————————————–
Distance moved by solvent

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14
Q

What is a trigylceride and what bond is made between 2

A

1 glycerol
3 fatty acids

Ester bond: O – C. 3H20 formed

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15
Q

What is Phospholids structure and function (Modified trigylceride)

A

2 fatty acids + glycerol + Phosphate group

Hydrophillic and phobic, —-> circle is phillic

Play a role in cell membrane

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16
Q

Uses of Trigylcerides

A

Energy source: Lots of H bonds, hydrolyse to release energy

Insulation : Traps air
Protection in body - Coats organs
Energy store; Insoluble, compact

17
Q

What are the main roles of lipids

A

Hormone production

  • membrane formation
  • Water proofing
  • Electrical Insulation - impulse transmission
18
Q

What is the amino acid general structure

A

N - C - C

R on top of C and O on right C

19
Q

What are the levels of structure of proteins

A

Primary structure: Seq of amino acids determined by DNA sequencd

Secondary structure: primary s is coiled or foiled - Alpha helix/ beta plated sheet

tertiary structure: Folding of secondary, 4 interactions…

Quaternary: Two or more polypeptide molecules to form 1 protein molecule

20
Q

Describe the 4 types of R group interactions

A

Hydrophillic/ Phobic - weak interactions between polar and non polar R groups

H bonds: Weakest bond form

Ionic bond : Stronger than H bonds, form oppositely charged R groups

Disulfide bridges : covalent, Strongest, only between r groups with sulfur atoms

21
Q

What is a macromolecule

A

Not made up of the same monomer