The Structure and Function of Large Biological Molecules: Chp 5 Flashcards Preview

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Flashcards in The Structure and Function of Large Biological Molecules: Chp 5 Deck (31)
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1
Q

polymers

A

long chain molecules made of repeating subunits called monomers EX: starch is a polymer composed of glucose molecules. EX2: proteins are polymers composed of amino acid monomers

2
Q

dehydration reactions

A

create polymrs from monomers. two monomers are joined by removing one molecule of water

3
Q

hydrolysis

A

occurs when water is added to split large molecules. this occurs in the reverse of dehydration reaction

4
Q

carbohydrates

A

include both simple sugars (glucose, fructose, galactose) and polymers such as starch made from these and other subunits. . All carbohydrates exist in a ratio of 1 carbon: 2 hydrogen: 1 oxygen

5
Q

monosaccharides

A

the monomers of carbohydrates. EX: glucose and ribose

6
Q

polysaccharides

A

polymers of monosaccharides EX: starch, cellulose, and glycogen

7
Q

functions of polysaccharides

A

energy storage and structural support

8
Q

energy-storage polysaccharides

A
  • starch is a storage polysaccharide found in plants

- glycogen is a storage polysaccharide found in animals, vertebrate muscle cells, and liver cells

9
Q

structural-support polysaccharides

A
  • cellulose is a majorcomponent of plant cell walls
  • chitin is found in the exoskeleton of arthropods, such as lobsters and insects and the cell walls of fungi. It gives cockroaches their “crunch”
10
Q

what type of molecules are lipids

A

they are hydrophobic. they are also NOT polyermes because they are assembled from a variety of components

11
Q

what are fats made up of

A

a glycerol molecule and three fatty acid molecules

12
Q

what are fatty acids composed of

A

hydrocarbon chains of variable lengths. the chains are nonpolar and therefore hydrophobic

13
Q

characteristics of saturated fatty acids

A

-have no double bonds between carbons
-tend to pack solidly at room temperature
-are linked to cardiovascular disease
-are commonly produced by animals
EX: butter and lard

14
Q

characteristics of unsaturated fatty acids

A

-have some carbond double bond that results in kinks
-tend to be liquid at room temperature
-commonly produced by plants
EX: corn oil and olive oil

15
Q

functions of lipids

A
  • energy storage (fats store twice as many calories/grams as carbs)
  • protection of vital orans and insulation
16
Q

characteristics of phospholipids

A
  • have a glycerol backbond (head), which is hydrophilic
  • have two fatty acid tails, which are hydrophobic
  • are arranged in a bilayer in forming the cell membrane, with the hydrophilic heads pointing toward the watery cytosol of extracellular environment, and hydrophobic tails sandwiched in between
17
Q

steroids

A

made up of four rings that are fused together

18
Q

cholesterol

A

a steroid. It is a common component of cell membranes

19
Q

estrogen

A

steroid hormone

20
Q

testosterone

A

steroid hormone

21
Q

proteins

A

polymers made up of amino acid monomers

22
Q

amino acids

A

contain a central carbon bonded to a carboxyl group, an amino group, a hydrogen atom, and an R group

23
Q

peptide bonds

A

link amino acids. formed by dehydration synthesis

24
Q

four levels of protein structure

A

primary structure is the unique sequence in which amino acids are joined. Secondary structure refers to one of two three-dimensional shapes that are the result of hydrogen bonding. Alpha helix are coiled shapes that appear like a slinky. Beta pleated sheets are accordion shaped. Tertiary structure results in a complex globular shape, due to interactions between R groups, such as hydrophobic interactions, van der waals interactions, hydrogen bonds, and disulfide bridges. globular proteins such as enzymes are held in position by the R group interactions. Quaternary structure refers to the association of two or more poly peptide chains into one large protein. Hemoglobin is a globular protein with quaternary structure, as it is composed of four chains.

25
Q

why is protein shape crucial to protein function

A

when a protein does not fold properly, its function is changed. This can be the result of a single amino acid substitution, such as that seen in the abnormal hemoglobin typical of sickle-cell disease

26
Q

chaperonins

A

protein molecules that assist in the proper folding of proteins within cells. they provide an isolating environment in which a polypeptide chain may attain final conformation

27
Q

what does it mean when a protein is denatured

A

when a protein is denatured it loses its shape and ability to function due to heat, a change in pH, or some other disturbance

28
Q

nucleic acids

A

DNA and RNA (their monomers are nucleotides)

29
Q

what are nucleotides made up of

A

nitrogenous base, pentose, and phosphate group

30
Q

characteristics of DNA

A
  • double-stranded helix
  • its nucleotides are adenine, thymine, cytosine, and guanine
  • adenine nucleotides will hydrogen bond to thymine nucleotides, and cytosine to guane
31
Q

characteristics of RNA

A
  • single stranded

- nucleotides are adenine, uracil, cytosine, and guanine