Module 2D

Question 1

which elements of CHNOPS pull on electrons more efficiently (more electronegtaive)

Answer 1

oxygen nitrogen and sulfur

Question 2

R groups rich in methyl; or carbon rings are

Answer 2

(C, H = nonpolar)

Question 3

are polar side chains hydrophobic or hydrphillic

Answer 3

hydrophillic

Question 4

are acidic side chains hydrophilic or hydrophobic

Answer 4

hydrophillic

Question 5

are carboxyl groups positive or negative charge

Answer 5

negative

Question 6

why is this amino acid considered acidic (proton donor) if it has a negative charge

Answer 6

carboxyl group (COOH) acts as an acid (can donate H+)

Question 7

is basic side chain hydrophobic or hydrophilic

Answer 7

hydrophilic

Question 8

how do electrically charged amino acids interact with water

Answer 8

favorably, via hydrogen bonding and ion-dipole interactions

Question 9

what facilitates the dissolution of amino acid in water

Answer 9

negatively charged oxygen atoms in water are attracted to the positively charged amino acid while the positively charged hydrogen atoms in water are attracted to the negatively charged amino acid

Question 10

what determines the function of the amino acid

Answer 10

structure

Question 11

confomration

Answer 11

spatial arrangement of atoms

Question 12

what does a functional protein consist of

Answer 12

one or more polypeptides twisted, folded, and coiled into a unique shape or conformation

Question 13

polypeptide backbone

Answer 13

amino acids minus side chains (R groups) connected by peptide bonds

Question 14

what atoms are included in the main chain or backbone of the proetin

Answer 14

alpha carbon, the carbonyl carbon, the amino nitrogen, and the carbonyl oxygen. the hydrogen atoms attached to the nitrogen and carbon atoms are also part of the backbone

Question 15

what is b sheet versus alpha helix dependent on

Answer 15

hydrogen bond

Question 16

tertiary

Answer 16

all proteins have tertiary structure but not all proteins have quaternary structure (multiple polypeptide chains)

Question 17

primary structure of a protein

Answer 17

unique sequence of amino acids

Question 18

what are the four levels of protein struture

Answer 18

primary, secondary, tertiary, and quaternary

Question 19

secondary structure

Answer 19

consist of cold and folds stabilized by H bonding of the polypeptide backbone

Question 20

alpha helix

Answer 20

right-handed helical structure formed by the hydrogen bonding between the carbonyl oxygen atom of one amino acid residue and the amide hydrogen atom of an amino acid located four residues ahead in the polypeptide chain

Question 21

what does beta sheet consist of

Answer 21

strands of polypeptides chains running alongside each other, with hydrogen bonds forming between adjacent strands. these hydrogen bonds occur between the carbonyl oxygen atom of one strand and the amide hydrogen atom of the adjacent strand

Question 22

tertiary structure

Answer 22

unique 3-dimensional shape stabilized by interaction among side chain (R group)

Question 23

grey strings

Answer 23

protein’s polypeptide chain that lack the repeating regularity of alpha helices or beta sheets

Question 24

what determines the tertiary structure

Answer 24

side chain interactions

Question 25

van der waals

Answer 25

attraction of intermolecular forces between molecules

Question 26

disulfide bridge

Answer 26

covalent links between the sulfur atoms of two cysteine amino acids

Question 27

ionic bond

Answer 27

formed from the electrostatic attraction between oppositely charged ions

Question 28

quaternary structure

Answer 28

Results when a protein consists of 2 or more polypeptides. Not all proteins have quaternary structures

Question 29

collagen

Answer 29

fibrous protein consisting of 3 intertwining polypeptides with identical alpha helices

Question 30

hemoglobin

Answer 30

contains four polypeptides subunits two of one kind (alpha) and two of another (beta)