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Biomolecules Flashcards

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1
Q

What is the chemical formula of glucose?

A

C6H12O6

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2
Q

What form does glucose exist as?

A

Either straight-chain or ring form

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3
Q

What are the types of glucose

A

Alpha glucose has its -OH below C-1
Beta glucose has its -OH above C-1

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4
Q

How are glycosidic bonds formed?

A
  • Condensation reaction
  • Between 2 monosaccharides
  • Removal of 1 water molecule
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5
Q

How are glycosidic bonds broken?

A
  • Hydrolysis reaction
  • Between 2 monosaccharides
  • Addition of 1 water molecule
  • Forms -OH group on both monosaccharides
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6
Q

What is starch made up of?

A

Amylose and Amylopectin

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7
Q

What is the structure of Amylose?

A
  • Alpha glucose
  • Alpha - 1, 4 - glycosidic bonds
  • Unbranched chain polymer
  • Coils into helical, compact structure
  • Stabilised by hydrogen bonds
  • -OH group on C-2 projects into helix
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8
Q

What is the structure of Amylopectin

A
  • Alpha glucose
  • Alpha - 1, 4 - glycosidic bonds and Alpha - 1, 6 - glycosidic bonds
  • Branched chain polymer
  • Coils into helical, compact structure
  • Stabilised by hydrogen bonds
  • -OH group on C-2 projects into helix
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9
Q

What are the properties of storage molecule?

A
  • Large and insoluble to not exert osmotic effect
  • Large so unable to diffuse out
  • Fold into compact shapes to store large amounts
  • Easily hydrolysed into monosaccharides
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10
Q

What is the function of starch?

A

Main energy storage molecule in plants

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11
Q

How does starch carry out its function?

A
  • Accumulates
  • Form starch grains
  • Stored in chloroplast
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12
Q

What makes starch/glycogen good at carrying out its function?

A
  • Compact structure so many glucose molecules can be stored
  • Readily converted back into glucose when needed
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13
Q

What is the structure of glycogen?

A
  • Alpha glucose
  • Alpha - 1, 4 - glycosidic bonds and alpha - 1, 6 - glycosidic bonds
  • Branched chain polymer
  • Coils into a helical, compact structure
  • Stabilised hydrogen bonds
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14
Q

What is the function of glycogen?

A

Main energy storage molecule in animals

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15
Q

How does glycogen carry out its function?

A
  • Accumulates
  • Form glycogen granules
  • Stored in liver/muscle cells
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16
Q

What is the structure of cellulose?

A
  • Beta glucose
  • Beta - 1, 4 - glycosidic bonds
  • Unbranched chain polymer
  • Straight chains of beta glucose run parallel to each other with numerous hydrogen bonds
  • Cellulose chains form bundles (microfibrils) which are arranged in larger bundles (macrofibrils)
  • Macrofibrils are interwoven and embedded in a gel-like matrix
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17
Q

What are the properties of cellulose?

A
  • Rigid
  • Insoluble
  • High tensile strength due to cross-linking
  • Long straight chains for formation of strong fibres
  • Unbranched polymers
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18
Q

What are the functions of cellulose?

A
  • Main component of the cellulose cell wall to provide structural support
  • Has large intermolecular spaces between macrofibrils to allow cell wall to be permeable
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19
Q

What is the structure of fatty acid chains?

A
  • Made up of a hydrophilic carboxyl group and a hydrophobic hydrocarbon chain
  • Either saturated or unsaturated
  • Saturated fatty acid chains consists of C-C bonds
  • Unsaturated fatty acid chains has at least one C=C bond
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20
Q

What are the properties of glycerol?

A
  • Soluble in water
  • -OH groups are hydrophilic
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21
Q

What are the properties of fatty acid chains?

A
  • Insoluble in water
  • C-H bonds are hydrophobic
22
Q

What is the structure of triglycerides?

A
  • 3 fatty acids chain and 1 glycerol molecule
  • Held together by 3 ester bonds
23
Q

What are the properties of triglycerides?

A
  • Fats are solid due to saturated fats allowing closer packing of fatty acid chains so more hydrophobic interactions form
  • Oils are liquid due to unsaturated fats causing kinks to prevent close packing of fatty acid chains so less hydrophobic interactions form
  • Soluble in organic solves
  • Insoluble in water
  • Able to be stored in large amounts without exerting osmotic effect
24
Q

What are the functions of triglycerides?

A
  • Respiratory substrate as the hydrocarbon chains can be hydrolysed and oxidised to produce energy in the form of ATP
  • Releases twice as much metabolic water compared to carbohydrates
  • Helps with buoyancy as it is less dense than water
  • Stored in adipose tissues to serve as a heat insulator
  • Adipose tissue is found around vital organs to protect them from physical impact
25
Q

What is the structure of phospholipids?

A
  • 1 phosphate group, 1 glycerol molecule and 2 fatty acid chains
  • Held together by 2 ester bonds and 1 phosphoester bond
26
Q

What are the properties of phospholipids?

A
  • Amphipathic as there is a hydrophilic phosphate head and hydrophobic fatty acid tails
  • Phosphate head is charged so it is soluble in water
27
Q

What are the functions of phospholipids?

A
  • Basic structure of the cell surface membrane
  • Forms the boundary between the cell and aqueous environment
  • Prevents ionic and polar molecules from entering cell
  • Forms micelles to help in the transport of fats from the guts to the liver
28
Q

What are the properties of amino acids?

A
  • Soluble in water to form zwitterions
  • Insoluble in organic solvents
  • Dipolar due to (+ and -) charged groups
  • Amphoteric due to basic and acidic group
  • Able to act as a pH buffer
29
Q

What are the four structures of proteins?

A

Primary, secondary, tertiary and quaternary

30
Q

What is primary structure?

A
  • Specific number and sequence of a.a
  • Joined by a peptide bond
  • In a p.p chain
31
Q

What is secondary structure?

A
  • Repeated coiling and folding of p.p chain
  • Maintained by hydrogen bonds between peptide bonds
32
Q

What are the types of secondary structures?

A

alpha helices & beta pleated sheets

33
Q

What are alpha helices?

A
  • Unbranched p.p chain
  • Tightly coiled into a spiral
  • Each turn is 3.6 a.a
  • Held together by intra-chain hydrogen bonding
34
Q

What are beta pleated sheets?

A
  • Extended adjacent regions of a p.p chain
  • Arranged in a parallel or antiparallel manner
  • Held together by hydrogen bonding
35
Q

What is tertiary structure?

A
  • Compact unique 3-D conformation
  • Further coiling and folding
36
Q

What are the types of bonds found in tertiary structure?

A
  • Hydrogen bonds
  • Hydrophobic interactions
  • Ionic bonds
  • Disulfide bonds
37
Q

What is quaternary structure?

A
  • More than 1 p.p chain
  • Held together by hydrogen bonds, ionic bonds, disulfide bonds and hydrophobic interactions
  • Between R-groups of different p.p chains
38
Q

What is denaturation?

A
  • Loss of specific 3-D conformation of a protein molecule
  • Involves the breakage of bonds
  • Proteins loses its structure and biological function
39
Q

What causes denaturation?

A
  • Temperature
  • pH-
  • Heavy metal ions
  • [R] / [O] agents
  • Organic solvents
40
Q

How does temperature affect proteins?

A
  • High temperature increases kinetic energy so atoms in proteins vibrate
  • Distrupts weak bonds
41
Q

How does pH affect proteins?

A
  • Changes in pH affects charged and polar R-groups
  • Distrupts ionic bonds and hydrogen bonds
42
Q

How does heavy metal ions affect proteins?

A
  • Positively charged
  • Form strong bonds with negatively charged carboxyl R-groups
    · Distrupts ionic bonds
    · With less negative charges, the solubility of the protein is reduced
43
Q

How do [R] / [O] agents affect proteins?

A
  • Distrupts disulfide bonds
  • Proteins loses their 3-D conformation
44
Q

How do organic solvents affect proteins?

A
  • Distrupts hydrogen bonding and hydrophobic interactions
45
Q

What is the nature of haemoglobin?

A
  • Responsible for transporting oxygen in the blood
  • Quaternary globular protein
  • 4 subunits
  • Each subunit has a p.p chain and a haem group
46
Q

What is the structure of the p.p chains in haemoglobin?

A
  • 2 identical α - chains
  • 2 identical β - chains
  • Each p.p chain is coiled into α - helices then folded into a globular shape
  • Hydrophobic amino acid on the interior
  • Hydrophilic amino acids on the exterior
  • Held together by hydrophobic interactions, ionic bonds and hydrogen bonds only
47
Q

What is the structure of the haem group in haemoglobin?

A
  • Porphyrin ring with an iron ion in the centre
  • Iron ion is able to bind to an oxygen molecule reversibly
  • Each haem group resides in a hydrophobic pocket
48
Q

What is the structure in relation to its function in haemoglobin?

A
  1. Hydropobic amino acids in the interior of the protein and hydrophilic amino acids found in the exterior serface of the protein to allow the haemoglobin molecule to be soluble
  2. The haem group is held in the hydrophobic pocket of the polypeptide chain to allow the haemoglobin to bind reversibly to oxygen and transport oxygen to the rest of the body
  3. Held together by weak bonds such as hydrophobic interactions, ionic bonds and hydrogen bonds to allow cooperative binding of oxygen to haemoglobin as haemoglobin will have to undergo conformational changes
  4. Haemoglobin is a globular protein so it is able to be compact and allows many haemoglobin to dissolve in one red blood cell
49
Q

What is the nature of collagen?

A
  • Fibrous protein
  • Performs structural and supportive function
  • Tropocollagen is the basic structural unit
  • Tropocollagen comprises of 3 polypeptide chains that wound around each other in a triple helix
50
Q

What is the structure of collagen?

A
  • Has a repeated triplet sequence of Gly - X - Y
  • Gly is glycine
  • X is usually proline
  • Y is usually hydroxyproline
  • Each of the three polypeptide chains are coiled into a helix
51
Q

What is the structure in relation to function of collagen?

A
  1. Every 3rd amino acid is glycine because it is the only amino acid small enough to fit in the centre so that the structure is compact
  2. Tropocollagen is held together by hydrogen bonds so that it is rigid
  3. Hydrophobic amino acids are found on the exterior surface so that it is insoluble in water and metabolically inactive, allowing it to be resistant to chemical changes
  4. Many triple helices lie parallel in a staggered pattern to form fibrils and with covalent bonds, fibrils unite to form fibres which allows collagen to have high tensile strength

Biology (1 decks)

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