The Structure of Amino Acids

Question 1

Functional groups

Answer 1

Small group of atoms bonded together in a precise configuration and exhibiting particular chemical properties that it imparts to any organic molecule in which it occurs.

Question 2

Phosphate group

Answer 2

A functional group characterized by a phosphorus atom bonded to 4 oxygen atoms, 3 single and one double bond. If the atom is not bonded to another atom its a phosphate ion. Has 2 negative charges in its oxygen atoms

Question 3

Carbonyl group

Answer 3

organic functional group composed of a carbon atom double bonded to an oxygen atom. Polar cause oxygen has a strong attraction for electrons

Question 4

Sulfhydryl group

Answer 4

Sulfur and hydrogen bond

Question 5

Carboxyl group

Answer 5

combination of two functional group attached to a single carbon atom, namely they’re hydroxyl (OH) and carboxyl (double bonded O) groups.

Question 6

Hydroxyl group

Answer 6

consists of an oxygen atom with two lone pairs bonding to a hydrogen atom. Participate in hydrogen bonding. R-OH

Question 7

Carbonyl group

Answer 7

chemically organic functional group composed of a carbon atom double bonded to an oxygen atom

Question 8

Carbon group

Answer 8

anything with carbon

Question 8

R group

Answer 8

Any group in which hydrogen or carbon atoms are attached to the rest of the molecule

Question 9

Macromolecules

Answer 9

Large molecules made from monomers

Question 10

Monomers

Answer 10

Molecular subunit used to build a macromolecule

Question 11

Polymer

Answer 11

Large number of monomers are bonded together

Question 12

Polymerization

Answer 12

Process by which many identical or similar small molecules (monomers) are covalently bonded to form a large molecule (polymer)

Question 13

Condensation reactions (DEHYDRATION)

Answer 13

Synthesis reaction and water leaves. Basuically 2 or more molecules combine to form a larger molecule and lose water.

Question 14

lysis

Answer 14

breakdown

Question 15

Hydrolysis

Answer 15

Opoosite reaction where the molecules rae broken down into two molecules. Water is invited to the party.

Question 16

amino acids

Answer 16

a small organic molecule with central carbon atom bonded to an amino group (-NH3), a carboxyl group (-COOH), a hydrogen atom, and a side chain

Question 17

Amino acid core structure

Answer 17

1.H-Hydrogen atom
2.NH2-An amino functional group
3. COOH-A carboxyl functional group
4. a distinctive “R-group” (side chain)

Question 18

R-Group (side chain)

Answer 18

Vary from single hydrogen atom to large structures containing carbon atoms linked into rings. Properties of amino acids vary because their R-groups vary.

Question 19

hydrophilic

Answer 19

Interacting readily with water. Typically polar compunds containing partially or fully charged atoms

Question 20

Hydrophobic

Answer 20

Not interacting readily with water.

Question 21

3 types of Amino acid R groups

Answer 21

Does the R-group have a negative charge? If so, it is acidic and has lost a proton, like aspartate.

Does the R-group have a positive charge? If so, it is basic and has picked up a proton, like lysine.

If the R-group is uncharged, does it have an oxygen atom? If so, then the highly electronegative oxygen will form a polar covalent bond in the R-group, thus making it uncharged polar like serine. (Although somewhat less electronegative, nitrogen atoms can also contribute polarity.) The overall polarity of an R-group is based on the number of highly polar covalent bonds relative to nonpolar bonds.

If it has neither a negative charge, positive charge or oxygen atom. It is a nonpolar amino acid

Question 22

Peptide bond

Answer 22

Covalent bond formed by condensation reaction between 2 amino acids.

Basically when carboxyl group reacts with the amino group of a second amino acid

Question 23

Peptide (oligopeptide)

Answer 23

A chain composed of fewer than 50 amino acid residues linked together by peptide bonds. Simply also referred to as peptuide.

Question 24

Polypeptides (many peptides)

Answer 24

Polymers that contain 50 or more amino acids linked by peptide bonds

Question 25

Residues

Answer 25

one amino acid

Question 26

Protein

Answer 26

Chain of amino acids

Question 27

primary structure

Answer 27

unique sequence of amino acids in a protein

Question 28

Secondary structure

Answer 28

local folded structures that form within a polypeptide due to interactions between atoms of the backbone. They’re stabilized largly by hydrogen bonding that occurs between the oxygen on the carbonyl group C–O of one amino acid residue and the hydrogen on the amino group N-H group of another.

Question 29

alpha helix

Answer 29

second structure in proteins formed when the polypetide backbone coils into a spiral shape stabilized by hydrogen bonding

Question 30

beta pleated sheet

Answer 30

segments of peptide chain bend 180 degrees than fold in the same plane. Secondary structure of proteins

Question 31

backbone

Answer 31

Refers to the polypeptide chain apart from the R groups

Question 32

Tertiary structure

Answer 32

Overall three dimensional shape of a single polypeptide. Form using a varoiety of bonds and intereactions between R-groups or between R-groups and the backbone.

Question 33

5 interactions involving R groups

Answer 33

Hydrogen bonding, Hydrophobic interactions, van der wals interactions, covalent bonds, ionic bonding

Question 34

Hydrogen bonding

Answer 34

Formed when a hydrogen bond is in between 2 highly electronegative atoms (F, N, O) in the same molecule

Question 35

Hydrophobic interactions

Answer 35

Interactions between nonpolar molecules in water and in their low solubility. Forces nonpolar sidechains together

Question 36

van der Waals interactions

Answer 36

weak intermolecular forces that happens when adjacent molecules are close together. Further stabilizes nonpolar sidechains and increase the stability of the protein

Question 37

Covalent bonding

Answer 37

equal sharing of electrons between 2 atoms to make them both stable.

Question 38

Disulfide bonds

Answer 38

Covalent bond between two sulfur atoms, typically in the side chains of certain amino acids.

Question 39

Ionic bonding

Answer 39

bonds that may form between groups that have full and opposing charges.

Question 40

Quaternary structure

Answer 40

Overall three deminsional shape formed from the combination of two or more polypetide chains.

Question 41

Macromolecular machines

Answer 41

Complexes of multiple proteins that assemble to carry out a particular function

Question 42

Denatured

Answer 42

unfolding or breaking up of a protein, modifies the standard three dimensional figure.

Question 43

Molecular chaperones

Answer 43

faciliates the folding or refolding of a protein into its correct three dimensional shape

Question 44

Prions

Answer 44

Proteinaceous infectious particles

Question 45

catalyst

Answer 45

Any substance that increases the rate of a chemical change without itself undergoing any permanent chemical change

Question 46

enzyme

Answer 46

protein that functions as a catalyst

Question 47

structural proteins

Answer 47

make up body components such as fingernails and hair

Question 48

Movement

Answer 48

Motor proteins and contractile proteins are responsible for moving the cell itself

Question 49

Signaling

Answer 49

Proteins are involved in carrying and receiving signals from cell to cell inside the body

Question 50

Transport

Answer 50

Proteins allow particular molecules to enter and exit cells or carry them throughout the body

Question 51

Defense

Answer 51

Proteins called antibodies attack and destroy viruses and bacteria that cause disease.

Question 52

Substrates

Answer 52

Reactant that interacts with a catalyst such as an enzyme in a chemical reaction