Chapter 28

Front 1

Unsaturated triaclyglycerols are usually-----because-----.

Back 1

liquids; kinks in fatty acid chains prevent fitting together closely

Front 2

two functional groups in all amino acids:

Back 2

carboxyl and amine

Front 3

fats and oils can be referred to by general term----because----

Back 3

triacylglycerols, they are formed by reaction of 1,2,3-propanetriol with three fatty acids

Front 4

in peptide Ala-Try-Gly-Phe, the N-terminal amino acid is

Back 4

alanine

Front 5

The tripeptide represented as ala-leu-gly is named

Back 5

Alanylleucylglycine

Front 6

which R group would most likely be found in hydrophobic area of tertiary structure of a globular protein?

Back 6

amide

Front 7

most naturally occuring monounsaturated fatty acids are classified as

Back 7

cis

Front 8

A ----protein extends completely through cell membrane

Back 8

integral

Front 9

a sphingolipid is

Back 9

an unsaturated amino alcohol

Front 10

the side chain for histidine is a ----r group. (basic, acidic...)

Back 10

basic

Front 11

the amino acid sequence of a protein is found in it's---structure

Back 11

primary

Front 12

the alpha helix of 2dary structure held together by -----bonds between two widely separated parts of protein chain

Back 12

hydrogen

Front 13

saponification involves-----reactions and the products are ---

Back 13

hydrolysis, glycerol and salt of fatty acid

Front 14

disulfide bonds in a protein chain connect

Back 14

two cysteine residues

Front 15

Is glycine chiral?

Back 15

no

Front 16

The lipid that is predominant in cell membranes is

Back 16

phospholipid

Front 17

----bonds combine amino acids in a protein.

Back 17

amide

Front 18

liquid veg oil is converted to solid fat by

Back 18

hydrogenation

Front 19

Triglycerides belong to which general classs of organic molecules?

Back 19

esters

Front 20

Bonds that are important in secondary structure of protein

Back 20

hydrogen

Front 21

fatty acids are ----acids with long, -----carbon chains.

Back 21

carboxylic, hydrophobic

Front 22

In a typical amino acid zwitterion, the carboxylate end is + or - charged?

Back 22

negative

Front 23

saponification reactions can be described as

Back 23

hydrolysis

Front 24

----amino acids are not synthesized in the body

Back 24

essential

Front 25

steroids are composed of

Back 25

tetracyclic ring with substituents at various position

Front 26

The alpha amino acid refers to

Back 26

molecule with amino group on alpha carbon

Front 27

hemoglobin is a -----with a ------structure

Back 27

protein, globular

Front 28

the addition of a base to a zwitteriion results in a ----charge on the carboxylate end and is also termed

Back 28

negative, anion (-)

Front 29

----acid is the immediate precursor to prostaglands and contains 20 carbons and 4 dble bonds

Back 29

arachidonic

Front 30

-----lipids give cell membranes shape

Back 30

glycerophospho

Front 31

fats are generally---at room temp and obtained from--

Back 31

solid, animals

Front 32

glycolipids are similar in structure to sphingomyelins except phosphate group has been replaced by a----

Back 32

carbohydrate

Front 33

the two main classifications of proteins are

Back 33

fibrous (structure) and globular (nonstructure)

Front 34

this lipid is the most abundant steroid in body and will give no fatty acid when hydrolyzed

Back 34

cholesterol

Front 35

lipids are hydrophobic. true or false

Back 35

true

Front 36

lipids are insoluble in water but solube in ---

Back 36

nonpolar solvent

Front 37

three major functions of lipids

Back 37

store energy, part of membranes, chemical messengers

Front 38

three energy-yielding substances

Back 38

fats, carbs, proteins

Front 39

the burning of ----produces twice as much energy as carbs

Back 39

fats at 9kcal/g, with carbs at 4

Front 40

simple lipids are

Back 40

fats, oils waxes

Front 41

list complex lipids and basic structure

Back 41

phopholipid- alc, fat acid, ester w/phosphate
sphingolipids-sphingosine, amide, unsaturated amino alcohol
glycolipid-sphingosine and carbohy

Front 42

solid fats have a---configuration

Back 42

trans

Front 43

glycerol is optically----

Back 43

inactive, no chiral carbon

Front 44

triglycerides, or triacylglycerols, are

Back 44

tri-esters of glycerol and carboxylic acids called fatty acids

Front 45

backbone of lipids----
long, hydrophobic carbon chains---

Back 45

backbone-glycerol
chains-fatty acid

Front 46

fatty acids contain an even # of unbranched carbons because

Back 46

they are mad up of acetate units

Front 47

unsaturated fatty acids in nature are almost always a ---isomer

Back 47

cis- prevents stacking and solidifying

Front 48

fats contain long, saturated fatty acids and therefore less dble bonds. true?

Back 48

true

Front 49

name two unsaturated fatty acids

Back 49

linoleic and linolenic acids

Front 50

hydrogenation is the addition of---

Back 50

h2

Front 51

when unsaturated fatty acids are converted from cis to trans, they increase this type of cholesterol

Back 51

LDL= low density lipoprotein (bad)

Front 52

prostaglandin functions include

Back 52

affect blood-platelet aggregation in clotting
-control inflam, lower blood pressure adn stimulate uterine contractions in childbirth

Front 53

waxes are esters with a long chain of carb acids with long chain alcs

Back 53

true

Front 54

glycerophospholipids are also called

Back 54

phosphoglycerlipids

Front 55

phospholipids contain

Back 55

alcohol, fatty acid and phospate groups

Front 56

glycolipids contain

Back 56

sphingosine as alc port., carbohydrate and fatty acid

Front 57

general function of membranes

Back 57

exclude dangerous chems while allowing nutrients in
confine special molecules to sections of cell

Front 58

membranes consist of

Back 58

hydrophillic, polar heads and hydrophobic, nonpolar tails

Front 59

---- is a type of transport that doesnt use energy

Back 59

facilitated diffusion

Front 60

the fat soluble vitamins are

Back 60

adek

Front 61

vit a good for
vit d for
vit k for

Back 61

a- vision
d- calcium metabolism
k- clotting

Front 62

water soluble vitamins assist in

Back 62

metabolism of enery-supplying nutrients

Front 63

proteins are digested to give

Back 63

amino acids

Front 64

functions of proteins (8)

Back 64

structure, catalysis, movement, transport, hormones, protection, storage, regulation

Front 65

there are --- amino acids that make up proteins in nature

Back 65

20 alpha amino acids

Front 66

neutral amino acids (15) have an equal # of amino and carb groups. acidic have more----than ----

Back 66

COOH than amino
they are aspartic acid and glut. acid

Front 67

the essential aa can be remembered by using PVT Tim Hall never argues(arg) and rarely tires (no tyr)

Back 67

they are arg, hist, isoleuc, leuc, lysine. methionione. phenly, threonin, tryptophan, valine

Front 68

all aa are chiral except

Back 68

glycine

Front 69

D and L indicate

Back 69

position of Nh2 in a fischer projection. D is on the RHS

Front 70

amphoteric means that an aa can react either as a

Back 70

base or acid

Front 71

aa exists mainly as -----, which can be altered to anion or cation with additon of base or acid, respectively

Back 71

zwitterions

Front 72

the pH of an aa is called

Back 72

isoelectric point (pI)

Front 73

buffer solutions neutralize both acids and bases. true?

Back 73

true

Front 74

at their pI, aa exist in aqueous solutions largely or entirely as

Back 74

zwitterion

Front 75

in proteins, the monomers are---and can also be called----because of the bonds between teh monomers

Back 75

amino acids, polypeptides or polyamides

Front 76

to form an amide bond between amino acids, an ----rxn of H20 must occur

Back 76

elimination

Front 77

polypeptides contain---- amino acids joined

Back 77

40-50

Front 78

in linear peptides, the amino group is called---terminal residue and carboxyl end i

Back 78

N, C terminal residue

Front 79

list 4 structures of protein and differences

Back 79

1- aa sequence
2-how segments of peptide backbone orient in pattern
3-how entire thing coils in 3d shape
4-how diff pros come togehter

Front 80

there are--------different dipeptides possible from the 20 aa. tripeptides? what is formula for figuring?

Back 80

20x20=400
20x20x20=8000
20n, n is #of peptides

Front 81

repeating patterns of proteins and the two most common

Back 81

2 structure,
alpha helix -coils with intramolecular h bonds
B-pleated sheet-backbone together with intermolecular hydrogen bonding

Front 82

tertiary structures are stabilized by (5)

Back 82

covalent (disulfide) bonds, h bonds, salt bridges (ionic) btwn acidicCOO- and basicNH3+, hydrophobic and metal ion coordination

Front 83

the 1 structure largely determines 2 and 3?

Back 83

yes

Front 84

examples of 4 structures

Back 84

hemoglobin and collagen (has 2 and 4)

Front 85

fibrous consist of ----structures and globular proteins of------structures

Back 85

2, 4

Front 86

conjugated proteins contain non-amino acid portions?

Back 86

yes

Front 87

the non-aa portion of conjugated protein is called

Back 87

prosthetic group.

ex- in hemoglobin, globins are non-aa and the heme units are prosthetics