The Structure and Function of Macromolecules

Question 1

polymer

Answer 1

a long molecule consisting of many similar or identical building blocks linked by covalent bonds

Question 2

monomers

Answer 2

small molecules; repeating units that serve as the building blocks of a polymer

Question 3

condensation reaction / dehydration reaction

Answer 3

monomers are connected by a reaciton in which two molecules are covalently bonded to each other through loss of a water molecule

Question 4

hydrolysis

Answer 4

monomers being broken by addition of water molecules; break with water; reverse of the dehydration reaction

Question 5

carbohydrates

Answer 5

include sugars and the polymers of sugars; monosaccharides, disacchaarides, polysaccharides

Question 6

classifying sugars

Answer 6

depending on the location of the carbonyl group (=C=O) -end: aldoses; middle: ketoses; size of the carbon skeleton: usually three to seven carbs long

Question 7

glycosidic linkage

Answer 7

covalent bond formel between two monosaccharides by a dehydration reaction

Question 8

glycogen

Answer 8

polysaccride; vertebrates store it mainly in liver and muscle cells

Question 9

cellulose

Answer 9

polysaccharide; major component of the tough walls that enclose plant cells

Question 10

alpha and beta glucose ring structures

Answer 10

differ in the placement of the hydroxyl group attached to the number 1 carbon

Question 11

starch 1-4 linkage of alpha glucose monomers

Answer 11

Question 12

cellulose: 1-4 linkage of beta glucose monomers

Answer 12

Question 13

fat

Answer 13

Fat is constructed from two kinds of smaller molecules: glycerol and fatty acids. Glycerol is an alcohol with three carbons, each bearing a hydroxyl group. A fatty acid has a long carbon skeleton, usually 16 to 18 carbon atoms in length. At one end of the fatty acid is a carboxyl group. function: energy storage, cushions, isolation

Question 14

phospholipid

Answer 14

Two fatty acids attached to glycerol.The third hydroxyl group of glycerol is joined to a phosphate group, which has a negative electrical charge. Additional small molecules, usually charged or polar, can be linked to the phosphate group to form a variety of phospholipids. hydrophilic heads, hydrophobic tails

Question 15

steroids

Answer 15

lipids characterized by a caron skeleton consisting of four rings

Question 16

cholesterol

Answer 16

steroid, is a common component of animal cell membranes and is also the precursor from which other steroids are synthesized

Question 17

proteins

Answer 17

speed up chemical reactions, structual support, storage, transport, cellular communication, movement, defense against foreign substances

Question 18

enzymes

Answer 18

regulate metabolism by acting as catalysts, chemical agents that selectively speed up chemical reactions in the cell without being consumed by the reaction

Question 19

enzymatic proteins

Answer 19

selective acceleration of chemical reactions

Question 20

structual proteins

Answer 20

support

Question 21

storage proteins

Answer 21

storage of amino acids

Question 22

transport proteins

Answer 22

transport other substances

Question 23

hormonal proteins

Answer 23

coordination of an organism’s activities

Question 24

receptor proteins

Answer 24

response of cell to chemical stimuli

Question 25

contractile and motor proteins

Answer 25

movement

Question 26

defense proteins

Answer 26

protection against disease

Question 27

polypeptides

Answer 27

polymers constructed from the same set of 20 amino acids. a protein consists of one or more polypeptides

Question 28

amino acid

Answer 28

At the center of the amino acid is an asymmetric carbon atom called the alpha carbon. It’s four different partners are an amino group, a carboxyl group, a hydrogen group and a variable group symbolized by R.

Question 29

peptide bond

Answer 29

covalent bond; When two amino acids are positioned so that the carboxyl group of one is adjacent to the amino group of the other, an enzyme can cause them to join by catalyzing a dehydration reaction, with the removal of a water molecule. amino end = N- terminus; carboxyl end = C- terminus; polypeptide backbone

Question 30

Frederick Sanger

Answer 30

pioneer in determining the amino acid sequence in proteins; approach: using protein- digesting enzymes and other catalysts that break polypeptides at specific places rather than completely hydrolyzing the chains to amino acids.

Question 31

primary structure

Answer 31

unique sequence of amino acids of a protein

Question 32

secondary structure

Answer 32

coils and folds (result of hydrogen bonds between the repeating constitutes of the polypeptide backbone) alpha helix: delicate coil held together by hydrogen bonding between every fourth amino acid; beta pleated sheet: two or more regions of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of the two parallel polypeptide

Question 33

tertiary structure

Answer 33

overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids; hydrophobic interactions: As a polypeptide fold into its functional conformation, amino acids with hydrophobic side chains usually end up in clusters at the core of the protein, out of contact with water. (exclude nonpolar substances). disulfide bridges: form where two cysteine monomers, amino acids with sulfhydryl groups (-SH) on their side chains, are brought close together by the folding of the protein.

Question 34

quaternary structure

Answer 34

the overall protein structure that results from the aggregation of these polypeptide subunits

Question 35

denaturation

Answer 35

If the pH, salt concentration, temperature, or other aspects of its environment are altered, the protein may unravel and lose its native conformation, a change called denaturation. It returns to its functional shape when the denaturating agent is removed.

Question 36

chaperonins (also called chaperone proteins)

Answer 36

protein molecules that assist the proper folding of other proteins, keep the new polypeptide segregated from bad influences PROCESS two proteins: one protein is a hollow cylinder, the othe is a cap that can fit on either end. 1.) an unfolded polypeptide enters the cylinder from one end 2.) the cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide 3.) cap comes off, and the prperly folded protein is released

Question 37

X-ray crystallography

Answer 37

an important method used to determine a protein’s 3D -structure. an X-ray beam through the crystallized protein; the diffracted X-ray expose photographic film, producing a pattern of spots known as X-ray diffraction pattern; examine amino acid sequence and 3D computer model

Question 38

nucleotide

Answer 38

3parts: nitrogenbase, pentose, phosphate group; without phosphate group it’s called a nucleoside

Question 39

pyrimide

Answer 39

nitrogen base, has a six-membered ring of carbon and nitrogen atoms, examples: cytosine, thymine, uracil

Question 40

purines

Answer 40

nitrogen bases; larger, with a six-membered ring fused to a five- membered ring, examples: adenine, guanine

Question 41

Watson and Francis Crick

Answer 41

proposed the double helix as a three dimensional structure of the DNA in 1953

Question 42

antiparallel

Answer 42

an arrangement, where two sugar-phosphate backbones run in opposite 5’ -> 3’ directions from each other