Biomolecules Flashcards

Unit 1 HL Y1 (49 cards)

1
Q

Hydrophobic

A

Lacking an affinity for water; unable to absorb, or be wetted by water

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2
Q

Hydrophilic

A

Having an affinity for water; able to absorb, or be wetted by water

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3
Q

What is a carbohydrate?

A

Carbohydrates are essential food nutrients. Your body turns carbs into glucose (blood sugar) to give you the energy you need to function.

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4
Q

Fructose

A

a sugar mostly found in honey and fruits.

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5
Q

Glucose

A

main sugar found in your blood

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6
Q

Galactose

A

A sugar in milk (and yogurt). It also contributes to energy production and storage in several human tissues.

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7
Q

Monosaccharides

A

Consists of a short chain of C- atoms. All carbohydrates contain monosaccharides in their structure.

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8
Q

Disaccharides

A

Disaccharides are two monosaccharides joined together

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9
Q

Sucrose

A

Common table sugar = Glucose + Fructose

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10
Q

Lactose

A

Major sugar in milk = Glucose + Galactose

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11
Q

Polysaccharides

A

Long chains of polymers covalently bonded.

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12
Q

Maltose

A

Product of starch digestion = Glucose + Glucose

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13
Q

Cellulose

A

Component of the cell wall

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14
Q

Starch

A

Found in plants. The most common are amylose and amylopectin.

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15
Q

osmosis

A

Osmosis is the movement of water molecules

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16
Q

Structural polysaccharides

A

Provide support. Make up structures.
EXAMPLE: Cellulose, Chitin

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17
Q

Storage polysaccharides

A

Store energy
EXAMPLE: Starch, Glycogen

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18
Q

Condensation

A

A reaction in which two molecules combine to form a larger molecule, producing a small molecule such as H2O as a byproduct.

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19
Q

How to draw a protein?

A

Label the amine group, carboxyl group, alpha carbon and R group on an amino acid.​

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19
Q

Hydrolysis

A

Hydrolysis is a reaction that uses up water molecules to break bonds.

20
Q

How many essential amino acids are there?

A

There are 9 essential amino acids

21
Q

What is the amino structure?

A

2 H’s and N then the central Carbon and a r group at the bottom and a hydrogen at the top, then the carboxyl group so, C double bonded with an O and then a bond with OH.

22
Q

Polypeptides

A

Two amino acid monomers aligned to form a peptide bond by condensation reaction.

23
Q

name the 3 fatty acids?

A
  1. unsaturated fats
  2. saturated fats
  3. trans fats
24
Dietary requirements for amino acids
Animal proteins have the nine essential amino acids our bodies need, whereas plant proteins don't contain them all within one source. Vegan diets require attention to food combinations to ensure essential amino acids are consumed.
25
Secondary structure
alpha (α): helix beta (β): sheets.
26
Primary
Unique sequence of AA in a protein Determined by genes Changes in this sequence alter the protein’s configuration (e.g. sickle-cell shape of hemoglobin Determination of AA sequence using Sanger’s Method
27
Secondary
Regular, repeating folding of a protein’s polypeptide backbone Stabilized by hydrogen between peptide linkages in the protein’s backbone (carbonyl and amino groups).
28
Tertiary Structure
Irregular contortions of a protein due to bonding between side chains (R-groups): superimposed upon primary and secondary structure
29
Covalent linkage
Disulfide bridges. Found when the amino acids contain sulfur. form between two cysteine monomers brought together by folding of the protein
30
Weak interactions
Hydrogen bonding Ionic bonds between charged side chains (cofactors + the R group) when the proteins contain cofactors Hydrophobic interactions between nonpolar side chains in protein’s interior
31
Hydrophobic Interactions
These amino acids orient themselves towards the center of the polypeptide to avoid the water
32
Disulphide Bridge
The amino acid cysteine forms a bond with another cysteine through its R group
33
Hydrogen Bonds
Polar "R" groups on the amino acids form bonds with other Polar R groups
34
Hydrophilic Interactions
These amino acids orient themselves outward to be close to the water
35
lonic Bonds
Positively charged R groups bond
36
Quaternary
Found in large globular proteins made up of more than one polypeptide Results from the interaction among several polypeptides (subunits) in a single protein.
37
Cysteine
Disulfide bridges form between two cysteine monomers bought together by folding of the protein. This is a strong bond that reinforces conformation.
38
What is the function lipids?
The functions of lipids include storing energy, signaling, and acting as structural components of cell membranes.
39
Fatty Acids
Joined by dehydration synthesis. Since there are three fatty acids attached, these are known as triglycerides
40
Structure of Fatty Acid
The “tail” of a fatty acid is a long hydrocarbon chain, making it hydrophobic. The “head” of the molecule is a carboxyl group which is hydrophilic.
41
Saturated Fats
A type of fat containing a high proportion of fatty acid molecules without double bonds, considered to be less healthy in the diet than unsaturated fat.
42
Unsaturated fats
A type of fat containing a high proportion of fatty acid molecules with at least one double bond, considered to be healthier in the diet than saturated fat.
43
Trans Fats
An unsaturated fatty acid is an arrangement of the carbon atoms adjacent to its double bonds. Consumption of such acids is thought to increase the risk of atherosclerosis.
44
Phospholipids
The phosphate group end of the molecule is hydrophilic because of the oxygens with all of their pairs of unshared electrons. This means that phospholipids are soluble in both water and oil.
45
osmosis
The movement of water from a higher concentration of water to a lower concentration of water.
46
hypertonic
The solution outside the cell contains a higher amount of concentration/salts, so the water leaves the cell, shrinking it
47
hypotonic
The solution outside the cell contains a lower amount of concentration/salts, so the water enters the cell, making it swell
48
isotonic
There is a balance of solutes and water molecules keeping an equilibrium