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Biology > Biological Molecules > Flashcards

Biological Molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Key properties of water

A 
. Liquid at room temp 
. Higher density in liquid state compared to solid 
. Upthrust Force
. Cohesive Properties 
. Adhesive Properties 
. Acts as a coolant 
. Polar molecule
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2
Q

What is a carbohydrates

A

Are a molecular compound which provide energy (short term) for functions such as regulation of blood glucose

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3
Q

What is the structural variation in alpha and beta glucose

A

In the alpha and beta glucose the OH (Hydroxyl group) group of carbon 1 is in opposite positions (alpha= above the plane, beta= below the plane)

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4
Q

How is a disaccharides formed?

A

. They form when two monosaccharide units join forming a glycosidic bond (condensation reaction)
. This can be from two of the same monosaccharides or two different ones
. For example glucose + fructose gives sucrose (and water)

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5
Q

What is a polysaccharide

A

. Is a molecule made up of multiple monosaccharides
. Is a slow release energy
. Examples would be cellulose, starch and glycogen

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6
Q

Properties of Starch

A
  • More soluble than glucose molecules
  • Has no taste or Oder
  • Energy store in plants
  • Example of starch would be Amylose (1,4 bond) and amylopectin (1,4 bond and glycosidic)
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7
Q

Properties of cellulose

A
  • Strong and insoluble
  • Is a straight molecule (not branched)
  • Make hydrogen bonds with each other
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8
Q

Properties of glycogen

A
  • Easy molecule for storage
  • Further Glucose molecules able to be added or removed
  • Insoluble and compact
  • Found in mainly liver and muscle cells
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9
Q

Definition of a polypeptide

A

A polypeptide is a chain of amino acids. Proteins are made up of one of more polypeptide chain

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10
Q

Characteristics of a Primary Protein Structure

A

. Straight chain of amino acids
. Particular amino acids in the chain influence how the polypeptide folds to give the final shape (Will determine function)
. Only bonds involved in the primary structure of a protein are peptide bonds

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11
Q

Characteristics of Secondary Structure(Alpha)

A

. Coil shape
. The oxygenw, hydrogen and nitrogen atoms of the basic, repeating structure of the amino acids interact
. Hydrogen bonds may form within the amino acid chain which pull it into a coil shape
. Hydrogen bonding every 4th amino acid

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12
Q

Characteristics of Secondary Structure (Beta)

A

. Sheet like structure joined by hydrogen bonds

. Pattern formed by the individual amino acid causes the structure to appear pleated

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13
Q

Characteristics of Tertiary Structure

A

. Folding of protein into its final shape
. Coiling or folding brings R-groups closer so they can interact and further coiling occurs
. Forms Hydrogen bonds, Ionic Bonds, Hydrophobic and Hydrophilic interactions and Disulphide bridges
. Looks like a backwards S

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14
Q

Characteristics of Quaternary Structure

A

. Made up of several polypeptide chains held together
. Same bonds as tertiary
. Forms a biologically active molecule
. Eg Haemoglobin

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15
Q

What is a phospholipid

A

. Are modified triglycerides
. Found in cytoplasm of each cell
. Negatively charged so soluble
. One fatty acid chain in a triglyceride molecule is replaced with a phosphate group to make a phospholipid

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16
Q

Saturated lipid

A

Only has C-C bonds
Found in animals fats and has a high MP
Eg lard

17
Q

UnSaturated lipid

A

Contains C=C bonds in the chain
Found in plant oils and have Low MP
They have a low MP due to having weak intermolecular forces of attraction

18
Q

Formation of a triglyceride

A

Glycerol + 3 Fatty Acids

19
Q

What is a Fibrous Protein

A

. Formed from large insoluble molecules
. Limited range of amino structure (small R-groups)
. Has an organised structure (Repetition of primary structure)
. Examples would be Keratin, Elastin and Collagen

20
Q

Globular Proteins

A

. Compact, water soluble and spherical
. Form when proteins fold into a tertiary structure (so amino acids are kept in an aqueous environment
. Solubility is important for many functions like regulation processes for life
. An example would be insulin

21
Q

Conjugated Proteins

A

. Are globular proteins containing a non-protein component called a prosthetic group
. An example of this would be Haem group. Contains an Iron (II) ion Fe2+
. Catalase and Haemoglobin contain a haem group
. Examples would be Catalase and Haemoglobin

22
Q

Keratin

A

. Present in hair and skin
. Contain large amount of sulphur (Reason burnt skin smells)
. Is a strong, inflexible and insoluble material (due to disulphide bond/bridges)

23
Q

Elastin

A

. Fibrous protein in elastic fibres
. Present in wall of blood vessels and alveoli
. Is a quaternary protein made from stretch molecules

Biology (15 decks)

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