Biological Molecules Flashcards by Soumya Saral

types of functional groups in carbohydrates (2)

aldehyde, ketone

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formula & shape of aldehyde group

CHO

O
||
C – H

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formula &shape of ketone group

C=O

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name of sugars containing ketone group

ketoses

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name of sugars containing aldehyde group

aldoses

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GLUCOSE

name of ring form

hexagonal 5-carbon pyranose ring

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GLUCOSE

aldose or ketose sugar?

aldose

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GLUCOSE

function

used to make ATP during respiration, animals

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GLUCOSE

mode of transport, animals

blood (dissolved in plasma)

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GLUCOSE

why is it easy to transport?

water-soluble

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FRUCTOSE

formula

C6H12O6

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FRUCTOSE

source

fruits

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FRUCTOSE

name of ring form

pentagonal 4-carbon furanose

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GLUCOSE

alpha glucose - diagram

OH is below the plane of the ring (on the right side):

H
 |
C
 |
OH

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GLUCOSE

beta glucose - diagram

OH is above the plane of the ring (on the right side)

OH
  |
 C
  |
 H

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FRUCTOSE

aldose or ketose?

ketose

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FRUCTOSE

why does it have same formula as glucose?

is an isomer

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GALACTOSE

formula

C6 H10 O6

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GALACTOSE

source

milk

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GALACTOSE

ring form

pyranose

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GALACTOSE

aldose or ketose?

aldose

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GALACTOSE

difference from glucose

OH on left side above the plane of the ring

OH
  |
 C
  |
 H

instead of

H
 |
C
 |
OH

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MALTOSE

reactant molecules

2 alpha glucoses

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MALTOSE

type of reaction that forms it

condensation

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MALTOSE | name of connecting bond

1,4 alpha-glycoside

SUCROSE | reactant molecules

alpha glucose & fructose

SUCROSE | type of reaction

condensation

SUCROSE | function

respiration in plants

SUCROSE | transport, plants

phloem sap (dissolved)

STARCH | function

energy storage, plants

STARCH | general formula

(C6 H12 O5)n

STARCH | polysaccharides

amylose, amylopectin

STARCH | ratio of amylose to amylopectin

1:4

AMYLOSE | % of starch

20%

AMYLOSE | monomer unit

alpha glucose

AMYLOSE | 2 features

unbranched chains | helical structure

AMYLOSE | linkage

1,4 alpha-glycosidic

AMYLOSE | reason for stability

H bonds

AMYLOPECTIN | % of starch

AMYLOPECTIN | monomer

alpha glucose

AMYLOPECTIN | structure

branched

AMYLOPECTIN | linkage

1,4 & 1,6 alpha glycosidic

AMYLOPECTIN | strength of hydrogen bonds

weak

AMYLOPECTIN | reason for reactivity

branched & unstable structure = easy to break bonds

AMYLOPECTIN | benefit of being in larger proportion than amylose

starch is easy to digest & break down

GLYCOGEN | general formula

(C6 H12 O5)n

GLYCOGEN | function

storage of sugar in animals

GLYCOGEN | how is it created?

glucose --> glycogen in presence of insulin

GLYCOGEN | structural features

highly branched

GLYCOGEN | monomer unit

alpha glucose

GLYCOGEN | linkages

1,4 & 1,6 alpha-glycosidic

GLYCOGEN | 3 benefits of using as a storage molecule in humans

highly branched = v. compact & easy to break down | insoluble in water

GLYCOGEN | benefit of being insoluble

osmotic potential of tissue fluid maintained; difficult to move around by accident (makes storage easy)

CELLULOSE | location

plant cell walls

CELLULOSE | monomer

beta glucose

``` CELLULOSE structure (4) ```

unbranched. straight chains, parallel to each other 180 degree face reversal of alternate glucose molecules v. strong hydrogen bonds

CELLULOSE | linkage

1,4 beta glycosidic

CELLULOSE | no. of glucose units in single chain

60-70

CELLULOSE | formation of cell wall (sequence)

chains -> microfibrils -> macrofibrils -> cell wall

monomers of lipids

glycerol; fatty acids

FATTY ACIDS | saturated

all C molecules are bonded to an atom; no free carbon molecules left

FATTY ACIDS | unsaturated

contain C=C

FATTY ACID | state at rtp (saturated)

solid

FATTY ACID | state at rtp (unsaturated)

liquid

TRIGLYCERIDES | reactant molecules

1 glycerol; 3 fatty acids

TRIGLYCERIDES | type of reaction

condensation

TRIGLYCERIDES | molecules of water formed

TRIGLYCERIDES | name of linkage

ester

TRIGLYCERIDES | advantage as an energy source

3x more energy derived than carbohydrates

TRIGLYCERIDES | disadvantage as an energy source

more difficult to break down

TRIGLYCERIDES | calorific value

36.4 kJ

TRIGLYCERIDES | use in plants (1)

formation of waxy cuticle to make leaves waterproof

TRIGLYCERIDES | use in animals (2)

production of metabolic water; thermal insulation

PHOSPOLIPIDS | structure

1 glycerol; 2 fatty acids; 1 phospate group

PHOSPOLIPIDS | properties

hydrophyllic ends facing in

PHOSPHOLIPIDS | composition

1 glycerol; 2 fatty acids; 1 phospate group

PHOSPHOLIPIDS | properties

hydrophilic heads | hydrophobic tails

PHOSPHOLIPIDS | arrangement in the cell membrane

bilayer; heads facing outwards O==O O==O O==O

PHOSPHOLIPIDS | types of fatty acids present in tail

unsaturated & saturated

PHOSPHOLIPIDS | impact of unsaturated fatty acids being present in bilayer

prevent the phospholipids from bunching too close together; the cell membrane remains fluid

CHOLESTROL | role in cell membrane (3)

1. regulates membrane fluidity by disrupting the regular pattern of phospholipids; 2. prevents close packing of phospholipids at low temperatures 3. limits uncontrolled leakage of small ions & water from the cell

CHOLESTROL | role in cell membrane (3)

PROTEINS | definition

organic compounds made of amino acids

AMINO ACIDS | definition

monomers of proteins

``` AMINO ACIDS groups present (2) ```

amine; carboxylic

AMINO ACIDS | formula of amine group

NH2

AMINO ACIDS | formula of carboxylic group

COOH

AMINO ACIDS | ways to classify (4)

essential/non-essential R group - present or absent acidity vs. basicity polarity

AMINO ACIDS | essential - meaning

not made in the body; have to be derived from other sources

AMINO ACIDS | non-essential - meaning

made in the body

AMINO ACIDS | which one doesn't have an R group?

glycine

AMINO ACIDS | what does glycine have instead of an R group?

AMINO ACIDS | shortest amino acid

glycine

AMINO ACIDS | cause for negative polarity

COOH group loses a hydrogen atom

AMINO ACIDS | cause for positive polarity

amine group gains a hydrogen atom

AMINO ACIDS | zwitter ion

charged amino acid whose overall polarity is zero

AMINO ACIDS | zwitter ion - formation

both amine & carboxylic groups gain & lose H atoms

AMINO ACIDS | acidic

R group contains COOH

AMINO ACIDS | basic

R group contains NH4

AMINO ACIDS | reaction through which they combine

condensation

AMINO ACIDS | name of linkage

peptide bond

AMINO ACIDS | name of peptide bond between two amino acids

dipeptide

AMINO ACIDS | name of peptide bond between three amino acids

tripeptide

POLYPEPTIDE | definition

a protein molecule made up of many amino acids linked to each other through a peptide bond

POLYPEPTIDE | reaction that breaks them down

hydrolysis

PROTEINS | where are they synthesised?

ribosome

PROTEINS | where are they synthesised?

ribosome

PROTEINS: PRIMARY STRUCTURE | primary structure - definition

linear sequence of amino acids in a polypeptide chain

PROTEINS: PRIMARY STRUCTURE | primary structure - linkage

peptide bonds

PROTEINS: PRIMARY STRUCTURE | how can it be broken?

hydrolysis/enzymes

PROTEINS: SECONDARY STRUCTURE | definition

structure that refers to the 3D arrangement of the main chain atoms

PROTEINS: SECONDARY STRUCTURE | how is it kept stable?

hydrogen bonds between molecules

PROTEINS: SECONDARY STRUCTURE | types (2)

alpha helix; beta-pleated sheet

PROTEINS: TERTIARY STRUCTURE | definition

structure that refers to the 3D arrangement of ALL the atoms in a protein

PROTEINS: TERTIARY STRUCTURE | types of bonds (4)

hydrogen; ionic; hydrophobic; disulfide

PROTEINS: TERTIARY STRUCTURE | types of bonds (4)

hydrogen; ionic; hydrophobic; disulfide bridges

PROTEINS: TERTIARY STRUCTURE | examples of strongly polar groups

--NH--, --CO--, --OH

PROTEINS: TERTIARY STRUCTURE | when can hydrogen bonds break?

at high temperatures & pH

PROTEINS: TERTIARY STRUCTURE | where do hydrophobic interactions occur?

between non-polar R groups

PROTEINS: TERTIARY STRUCTURE | why do hydrophobic groups stay together?

are repelled by water env. around them

PROTEINS: TERTIARY STRUCTURE | where do ionic bonds form?

between ionized amine and carboxylic groups

PROTEINS: TERTIARY STRUCTURE | how can ionic bonds be broken?

by changes in pH

PROTEINS: TERTIARY STRUCTURE | diff. b/w ionic & hydrogen bonds

hydrogen: form between partially charged groups ionic: form between fully ionised groups

PROTEINS: TERTIARY STRUCTURE | between which amino acids does a disulfide bridge form?

cysteine

PROTEINS: TERTIARY STRUCTURE | element involved in disulfide bridges

sulphur

PROTEINS: TERTIARY STRUCTURE | how can disulfide bridges be broken?

by a reducing agent (2H removed)

PROTEINS: TERTIARY STRUCTURE | arrangement of bonds acc. to strength (weak to strong)

hydrophyllic < hydrogen < ionic < disulfide

PROTEINS: TERTIARY STRUCTURE | arrangement of bonds acc. to strength (weak to strong)

hydrophobic < hydrogen < ionic < disulfide

PROTEINS: TERTIARY STRUCTURE | molecules in a fibrous protein: shape

long and thin

PROTEINS: TERTIARY STRUCTURE | molecules in a fibrous protein: arrangement

rows, parallel to each other (form fibrils)

PROTEINS: TERTIARY STRUCTURE | molecules in a fibrous protein: solubility

not soluble in water

PROTEINS: TERTIARY STRUCTURE | fibrous proteins - role: structural or metabolic?

stuctural

PROTEINS: TERTIARY STRUCTURE | fibrous proteins: 2 examples + location

collagen: outer walls of arteries & veins keratin: hair and fingernails

PROTEINS: COLLAGEN | no. of polypeptide chains

3 (triple helical)

``` PROTEINS: COLLAGEN primary structure (2) ```

repetitive sequence of amino acids; every 3rd amino acid is glycine

PROTEINS: COLLAGEN | which bond stabilises the structure?

H--H

PROTEINS: COLLAGEN | main function

to provide support & elasticity in animal tissues

PROTEINS: COLLAGEN | reason for insolubility

molecules too large and long to dissolve in water

PROTEINS: COLLAGEN | benefit of having 3 polypeptide chains

high tensile strength

PROTEINS: COLLAGEN | meaning of high tensile strength

can stretch slightly & withstand large pulling forces without breaking

PROTEINS: COLLAGEN | benefit of having glycine as a repeating unit

compactness = chains pack together strongly

PROTEINS: COLLAGEN | role of lysine

formation of cross-links between molecules = formation of fibrils & fibres of collagen

PROTEINS: GLOBULAR PROTEINS | shape

spherical

PROTEINS: GLOBULAR PROTEINS | arrangement of molecules

hydrophobic amino acids face inwards; hydrophobic amino acids face outwards

PROTEINS: GLOBULAR PROTEINS | solubility

soluble

PROTEINS: GLOBULAR PROTEINS function: structural or metabolic?

metabolic

PROTEINS: GLOBULAR PROTEINS | examples + location

Hb - blood | salivary amylose - salivary gland/mouth

Biological Molecules Flashcards

(147 cards)