BioChem Flashcards

PreBoards

1
Q

Naturally occur in living organisms and consist mostly of
carbon, hydrogen, oxygen and nitrogen

A

BIOMOLECULES

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2
Q

Essential for various body functions & manufactured
within the body

A

BIOMOLECULES

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3
Q

Heterogenous group of organic compounds that are
insoluble in water and soluble in nonpolar organic
solvents.

A

LIPIDS

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4
Q

Nonpolar organic solvents

A

Diethyl ether
Acetic acid (very common)
Benzene
Hexane
CCl4 (Carbon tetrachloride)
Ethyl acetate
Chloroform

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5
Q

An important source of energy

A

LIPIDS

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6
Q

Naturally occur in most plants, microorganisms and
utilized as components of the cell membrane, energy
storage molecules, insulation and hormones.

A

Lipids

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7
Q

Glycerol + Fatty Acid

A

Lipids

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8
Q

Sparingly insoluble or insoluble but soluble in organic
solvents

A

Lipids

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9
Q

Lipids make up the membrane of the cell called

A

Lipid bilayer

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10
Q

Energy-rich molecules mostly made up of hydrocarbons.

A

Lipids

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11
Q

Fatty acids, glycerol, sphingosine, and sterol are its
primary building blocks

A

Lipids

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12
Q

Fat cells known as

A

Adipocytes

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13
Q

Compose the basic structure of all cell membranes (3)

A

Phosphoglycerides, sphingolipids and steroids

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14
Q

Monomer of Lipid

A

Fatty acid

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15
Q

Fatty Acids with a carbon chain in which all carbon-carbon bonds are single bonds

A

SATURATED FATTY ACIDS

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16
Q

Fatty acids with a carbon chain in which there is a
presence of one carbon-carbon double bond

A

MUFAs

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17
Q

Fatty acids with a carbon chain in which there is a
presence of 2 or more carbon-carbon double bond

A

PUFAs

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18
Q

When carbon chain length increases, solubility

A

decreases

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19
Q

Carbon chain length and the number of double bonds
present / degree of unsaturation determines a fatty
acid’s

A

melting point

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19
Q

Unsaturated fatty acid - Melting point decreases as
degree of unsaturation

A

increases

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20
Q

Energy-storage lipids

A

(Triacyglycerols)

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20
Q

Saturated fatty acid - Carbon length increases,
melting point

A

increases

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21
Q

Membrane Lipids

A

Phospholipids, Sphingoglycolipids, Cholesterol

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22
Q

Emulsification Lipids

A

Bile Acids

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23
Q

Messenger Lipids

A

Steroid Hormones and
Eicosanoids

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24
Q

Lipid formed by the esterification of three FA to a
glycerol molecule

A

Triacylglycerols (TAGs)

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25
Q

Protective Coating Lipids

A

Biological Waxes

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26
Q

Mostly concentrated primarily in special cells known as
Adipocytes

A

Triacylglycerols (TAGs)

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27
Q

Efficient at storing energy compared to glycogen
because large quantities can be packed into a very
small volume

A

Triacylglycerols (TAGs)

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28
Q

Most Abundant type of lipid in the body

A

Triacylglycerols (TAGs)

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28
Q

Triester formed from the esterification of glycerol with
more than one kind of fatty acid molecule.

A

Mixed Triacylglycerol

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29
Q

Most biochemically important to TAGs and mixed TAG

A

Mixed Triacylglycerol

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30
Q

Semi-solid at room temperature

A

Fats

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31
Q

Generally obtained from animal sources: “animal fat”

A

Fats

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32
Q

Liquid at room temperature

A

Oils

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33
Q

Generally obtained from plant sources

A

Oils

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34
Q

Functions almost exclusively as components
of the cell membrane and are not stored

A

Glycerophospholipids

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35
Q

most abundant type of
membrane lipid

A

Phospholipids

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36
Q

A polar class of lipids

A

Glycerophospholipids

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37
Q

Also known as Lecithins

A

Phosphatidylcholines

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38
Q

Prevalent in cell membranes

A

Phosphatidylcholines

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39
Q

Waxy solid that form colloidal suspensions in water

A

Phosphatidylcholines

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40
Q

Dietary sources: Egg yolks and soybeans

A

Phosphatidylcholines

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41
Q

Also known as Cephalins

A

Phosphatidyethanolamines and phosphatidylserines

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42
Q

Lipids that contain one fatty acid and one phosphate
group attached to a sphingosine molecule and an
alcohol attached to a phosphate group

A

Sphingophospholipids

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43
Q

Found in all cell membranes and are important
structural component of the myelin sheath

A

Sphingomyelins

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43
Q

Sphingophospholipids in which the alcohol esterified to
the phosphate group is choline

A

Sphingomyelins

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44
Q

Presence of amide and glycosidic linkages

A

Sphingoglycolipids

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45
Q

Lipids that contain one fatty acid and one phosphate
group attached to a sphingosine molecule

A

Sphingoglycolipids

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46
Q

Simplest sphingoglycolipids

A

Cerebrosides

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46
Q

A C27 steroid molecule that is a component of cell
membranes and a precursor for other steroid – base
lipids

A

CHOLESTEROL

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46
Q

Can undergo saponification reaction

A

Sphingoglycolipids

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47
Q

Occur primarily in the brain

A

Cerebrosides

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48
Q

Occurs both in the gray matter of the brain, as well as
the myelin sheath

A

Gangliosides

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49
Q

Most abundant steroid in the human body

A

CHOLESTEROL

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50
Q

Serves as a precursor for several other important
steroid molecules

A

CHOLESTEROL

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51
Q

carry cholesterol from the liver to various
tissues

A

Low density lipoprotein (LDL)

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52
Q

“bad cholesterol”

A

Low density lipoprotein (LDL)

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53
Q

Carry excess cholesterol from tissues back to the liver

A

High density lipoprotein (HDL)

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54
Q

“good cholesterol”

A

High density lipoprotein (HDL)

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55
Q

Also known as “plasma membrane” because it is
responsible for separating the cytoplasm of a cell form
its surroundings.

A

Cell Membrane

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56
Q

A lipid-base structure that also controls the movement
of substance into and out of the cell

A

Cell Membrane

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57
Q

Upto 80%of the mass of a cell is lipid material consisting primarily of the three types of membrane lipids:

A

➔ Phospholipids
➔ Glycolipids
➔ Cholesterol

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58
Q

components of cell
membranes and they provide rigidity to the membrane

A

Cholesterol molecules

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59
Q

membrane protein
- Penetrates the cell membrane

A

Integral membrane protein

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60
Q

No energy is required Transport process

A

Passive Transport & Facilitated Transport

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60
Q

membrane protein
- Nonpenetrating membrane protein located
on the surface of the cell membrane.

A

Peripheral membrane protein

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61
Q

Transport process in which a substance moves across
a cell membrane by diffusion from a region of higher
concentration to a region of lower concentration

A

Passive Transport

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62
Q

● Transport process in which a substance moves across
a cell membrane, with the aid of membrane proteins
● Movements is from the higher concentration to a lower
concentration

A

Facilitated Transport

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62
Q

Transport process in which a substance moves across
a cell membrane, with the aid of membrane proteins,
against a concentration gradient

A

Active transport

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63
Q

Energy is required Transport process

A

Active transport

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64
Q

A derivative of cholesterol that functions as a lipid-emulsifying agent in an aqueous environment of the
digestive tract

A

Bile acids

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65
Q

A substance that can disperse and stabilize water insoluble substances as colloidal particles in an aqueous solution

A

Emulsifiers

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66
Q

Carries an amino acid attached to the side-chain carboxyl group with the aid of an amide linkage

A

Bile acids

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67
Q

A fluid that contains emulsifying agents secreted by the liver, stored in the gallbladder, and released into the small intestine during digestion

A

Bile

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68
Q

A biochemical substance that serves as a means of
communication between various tissues

A

Hormone

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69
Q

Produced by a ductless gland

A

Hormone

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70
Q

Control the balance of Na+ and K+ ions in cells and body fluids

A

Mineralocorticoids

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70
Q

A hormone that use cholesterol derivative

A

Steroid Hormone

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71
Q

Major classes of steroid hormones
- Regulate numerous biochemical process in the body

A

Adrenocorticoid hormone

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71
Q

Major classes of steroid hormones
- Control reproduction and
secondary sex characteristics

A

Sex hormones

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72
Q

Major mineralocorticoid

A

Aldosterone

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73
Q

○ Control glucose metabolism
○ Counteract inflammation

A

Glucocorticoid

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74
Q

metabolic precursor for most
eicosanoids

A

Arachidonic acid

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75
Q

Major glucocorticoid

A

Cortisol

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75
Q

➔ Synthesized in the largest amount by adrenal glands
➔ Exert powerful anti-inflammatory effects in the body

A

Cortisol

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76
Q

Hormone – like molecules because they are not
transported in the bloodstream to their site of action.
Their effects are exerted in the tissues where they are
synthesized

A

Eicosanoids

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77
Q

Have a very short “life”, as they are broken down into
inactive residues within seconds of synthesis

A

Eicosanoids

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78
Q

a monoester of a long-chain fatty acid and a long-chain
alcohol

A

Biological Wax

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79
Q

saturated fatty acids are present (may contain 14 – 36
carbon atoms)

A

Biological Wax

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80
Q

Alcohols found in biological waxes may either be
saturated or unsaturated (may contain 16 – 30 carbon
atoms)

A

Biological Wax

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81
Q

Weak polar head and 2 long nonpolar trails

A

Biological Wax

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82
Q

Salkowski’s test

A

bluish red to purple

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83
Q

Liebermann Burchard test

A

(+) = red or pink-> purple- >blue -> bluish – green colour.

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84
Q

uses acetic anhydride and sulfuric acid

A

Liebermann Burchard test

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85
Q

contains one amino group , one carboxyl group, and a
nonpolar side chain

A

Nonpolar Amino Acid

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85
Q

MOST ABUNDANT molecules in
the cells after water

A

PROTEINS

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86
Q

An organic compound that contains both amino (-NH2)
and carboxyl (-COOH) groups attached to the same
Carbon atom

A

AMINO ACIDS

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87
Q

an amino acid that contains one amino group, one
carboxyl group, and a side chain that is polar but
neutral

A

Polar Neutral Amino Acid

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88
Q

an amino acid that contains one amino group and two
carboxyl groups, the second carboxyl group being part
of the side chain.

A

Polar Acidic Amino Acids

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89
Q

the side chain of a polar
acidic amino acid bears
a ________ charge

A

negative

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90
Q

an amino acid that contains two amino groups and one
carboxyl group, the second amino group being part of
the side chain.

A

Polar Basic Amino Acid

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91
Q

A molecule that has a positive charge on one atom and
a negative charge on another atom, but which has no
net charge

A

ZWITTERIONS

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91
Q

the -NH3 of the zwitterion loses a proton, and a negatively charged species is formed

A

In basic solution

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91
Q

the zwitterion accepts a proton
to form a positively charged ion Zwitterions

A

In an acidic solution

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92
Q

Unbranched chain of Amino Acids

A

PEPTIDES

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92
Q

Chain of covalently linked amino acids

A

PEPTIDES

93
Q

love hormone

A

OXYTOCIN

93
Q

A covalent bond between the carboxyl group of one
amino acid and the amino group of another amino acid

A

Peptide bond

94
Q

plays a role in stimulating the flow of milk in a nursing mother

A

OXYTOCIN

95
Q

regulates uterine contractions & lactation

A

OXYTOCIN

96
Q

regulates the excretion of water by the kidneys

A

VASOPRESSIN

97
Q

The hydrogen bonding present is intramolecular

A

ALPHA HELIX

97
Q

are pentapeptide neurotransmitters produced
by the brain and bind at receptor sites within
the brain

A

Enkephalins

97
Q

occurs when there are two nonpolar side chains
close to each other

A

Hydrophobic Interactions

97
Q

The overall three-dimensional shape of a protein that
results from the interactions between amino acid side
chains (R groups) that are widely separated from each
other within a peptide chain.

A

TERTIARY STRUCTURE

97
Q

Compact spherical molecules that are usually water soluble.

A

Globular Proteins

97
Q

proteins whose molecules have peptide chains that are folded into spherical or globular shapes

A

Globular Proteins

97
Q

Can undergo denaturation

A

Globular Proteins

97
Q

A protein secondary structure in which two fully
extended protein chain segments in the same or
different molecules are held together by hydrogen
bonds.

A

BETA - PLEATED SHEETS

97
Q

also known as Antidiuretic Hormone (ADH)

A

VASOPRESSIN

97
Q

can also affect blood pressure

A

VASOPRESSIN

97
Q
  • also known as Salt Bridges
  • always involved in the interaction between an acidic and basic side chain
A

Electrostatic Interactions

97
Q
  • can occur between amino acids with polar R groups
  • relatively weak and easily disrupted by changes in
    the pH and temperature
A

Hydrogen Bonds

97
Q

antioxidant and protects
cellular contents from oxidizing agents

A

GLUTATHIONE (Glu-Cys-Gly)

97
Q

Protein secondary structure in which a single protein
chain adopts a shape that resembles a coiled spring

A

ALPHA HELIX

98
Q

The hydrogen bonds can either be intermolecular
or intramolecular

A

BETA - PLEATED SHEETS

98
Q

the strongest of the tertiary- structure interactions, result from the - SH groups of two cysteine residues reacting with each other to form a covalent disulfide bond

A

Covalent Disulfide bonds

99
Q

Function as enzymes and intracellular signaling
molecules

A

Globular Proteins

99
Q

Organization among the various peptide chains in a multimeric protein

A

Quaternary structure

99
Q
  • found in hair , wool, skin, horns & fingernails
  • provide protective coating for organs
  • mainly made up of hydrophobic amino acid residues rendering them insoluble in water
A

Keratin

99
Q

involved in iron transport in
blood

A

Transferrin

99
Q

regulatory hormone for controlling
glucose metabolism

A

Insulin

99
Q

Involved in oxygen storage in
muscles

A

Myoglobin

99
Q

found in blood vessels and ligaments

A

Elastins

99
Q

● protein whose molecules have an elongated shape
with one dimension much longer than the others.
● have simple, regular and linear structures
● such proteins have the tendency to aggregate together
to form macromolecular structures
● provide support and & external protection

A

Fibrous Proteins

99
Q

involved in immune
system responses

A

Immunoglobulins

99
Q

found in muscle tissue

A

Myosins

99
Q

found in blood clots

A

Fibrin

99
Q
  • most abundant protein in the human body - major
    structural material in tendons, ligaments, blood vessels
    and skin
  • organic component of bones and teeth
  • Vit. C is needed for the synthesis
A

Collagen

99
Q

● Is a disease that arise due to an inadequate diet and starvation.
● actually the result of a lack of protein in the diet.
● it is an acute form of childhood protein-energy malnutrition

A

Kwashiorkor

100
Q
  • also known as Beta- keratin
  • consists of small amino acid residue
A

Silk Fibroin

100
Q

Involves the disruption and possible destruction of both the secondary and tertiary structures of a protein.

A

Denaturation

100
Q

deficiency of collagen-processing-enzymes, or from mutations in the amino
acid sequences of collagen
types I, III or V.

A

Ehler’s - Danlos syndrome

100
Q

● Is also a heterogenous group of inherited disorders distinguished by bones that easily bend and fracture.
● Common features: retarded wound healing and a rotated and twisted spine leading a hump-back appearance

A

Osteogenesis Imperfecta

100
Q

● Is a form of severe protein- energy malnutrition characterized by energy deficiency.
● caused by severe deficiency of nearly all nutrients, especially protein and carbohydrates

A

Marasmus

100
Q

small organic molecule that serves as a cofactor in a conjugated enzyme

A

Coenzyme

100
Q

Mutations in the Type II Collagen

A

Osteogenesis
imperfecta congenita

100
Q

the active site in the enzyme has a fixed, rigid geometrical conformation. Only substrates with a complementary geometry can be accommodated at such a site, much as a lock accepts only certain keys

A

LOCK-AND-KEY MODEL

100
Q

Also known as Brittle bone syndrome

A

Osteogenesis Imperfecta

100
Q

Mutations in the Type I Collagen

A

Osteogenesis
imperfecta tarda

100
Q

the inactive form of apoenzyme

A

proenzyme / zymoge

100
Q

protein part of the conjugated enzyme

A

Apoenzyme

100
Q

an enzyme with absolute specificity. It catalyzes the - conversion of hydrogen peroxide (H2O2) to O2 and H2O. Hydrogen peroxide is the
only substrate it will accept

A

Catalase

100
Q

biochemically active conjugated enzyme produced from an apoenzyme & a cofactor

A

Holoenzyme

101
Q

allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate. A good analogy is the changes that occur in the shape of a glove when a hand is inserted into it.

A

INDUCED - FIT MODEL

101
Q

it adapts to accept the incoming substrate

A

INDUCED - FIT MODEL

101
Q

group-specific; it leaves amino acids, one at a time, from the carboxyl end of a peptide chain

A

Carboxypeptidase

101
Q

temperature at which an
enzyme exhibits maximum activity

A

Optimum temperature

101
Q

a molecule that inactivates enzymes by forming a
strong covalent bond to an amino acid side-chain group
at the enzyme’s active site.

A

Irreversible inhibitor

102
Q

hydrolyze phosphate-ester bonds in all types of phosphate esters

A

Phosphatases

102
Q

slows or stops the normal catalytic function of an
enzyme by binding to it

A

Enzyme Inhibitor

102
Q

pH at which an enzyme exhibits
maximum activity

A

Optimum pH

103
Q

A molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can compete with the substrate for occupancy of the enzyme’s active site.

A

Competitive inhibitor

103
Q

Major function: components of
coenzymes

A

B vitamins

103
Q

A molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site.

A

Noncompetitive inhibitor

103
Q

produced in the skin of humans and animals by the action of
sunlight (ultraviolet light) on its precursor molecule

A

Vitamin D3

104
Q

combines with opsin
protein to form the visual pigment rhodopsin which further converts light energy into nerve impulses that are sent to the brain

A

VITAMIN A

104
Q

co-substrate in the formation of structural protein collagen

A

VITAMIN C

104
Q

A three-subunit molecule in which a pentose sugar is bonded to both a phosphate group and a nitrogen-containing heterocyclic base

A

NUCLEOTIDES

104
Q

Biomolecules that store and transmit genetic information in the cells
Main function: Storage and expression of genetic information

A

NUCLEIC ACIDS

104
Q

Primary function: Antioxidant – protects against oxidation of other compounds

A

VITAMIN E

104
Q

Active in the formation of proteins involved in regulating blood clotting

A

VITAMIN K

104
Q

○ Adenine
○ Guanine

A

Purine Derivatives

104
Q

● primary structure of a nucleic acid
● sequence in which nucleotides are linked together in a nucleic acid

A

Nucleotide Sequence

105
Q

Known as the “Working Copies” of DNA

A

RIBONUCLEIC ACID

105
Q

Chemical basis of heredity & considered as
the fundamental units of genetic information

A

DEOXYRIBONUCLEIC ACID

105
Q

○ Thymine
○ Cytosine
○ Uracil

A

Pyrimidine Derivatives

105
Q

A biological process that occurs in all living organisms
and copies their DNA ; this is the basis for biological
inheritance

A

REPLICATION

105
Q

● The flow of information from DNA to RNA to protein
● DNA is the repository and directs its own replication
● DNA is transcribed into RNA
● mRNA is translated into a polypeptide gene product

A

CENTRAL DOGMA

105
Q

ENZYMES involved: unwinds the supercoils

A

Topoisomerases

106
Q

ENZYMES involved: unwinds the DNA double helix

A

DNA helicase

106
Q

ENZYMES involved: join lagging strand together

A

DNA ligase

106
Q

This is a process known to produce new DNA
molecules

A

REPLICATION

106
Q

The copying process, during which a DNA strand
serves as a template

A

TRANSCRIPTION

107
Q

enzyme responsible for copying DNA templates

A

DNA polymerase

107
Q

components of ribosomes, the complexes that carry out the synthesis of proteins

A

rRNA

107
Q

ENZYMES involved: works on 5’ - 3’ direction only

A

DNA polymerase

107
Q

intermediaries, carrying genetic information from one or a few genes to a ribosome

A

mRNA

108
Q

these are the stop signals

A

UAG, UAA, and UGA

108
Q

start codon

A

AUG

108
Q

adapter molecules
that faithfully translate the information in mRNA into a specific sequence of amino acids.

A

tRNA

109
Q

three letter word, that contains the information necessary for the synthesis of proteins

A

CODON

110
Q

provides the template or blueprint for this process.

A

Messenger RNA

110
Q

process when mRNA carries coded information to ribosomes

A

TRANSLATION

111
Q

The altered information can cause changes in amino
acid sequence during protein synthesis and thereby
after protein function.

A

MUTATION

111
Q

Errors in genetic information is passed on during transcription

A

MUTATION

112
Q

An error in base sequence reproduced during DNA replication.

A

MUTATION

112
Q

there is a change but the protein still codes for the same amino acid. There is no manifestation to the individual

A

SILENT MUTATION

113
Q

A different codon is produced therefore it codes for a different amino acid

A

MISSENSE MUTATION

113
Q

An inherited blood disorder that affects the shape of the red blood cells (a flawed hemoglobin)

A

SICKLE-CELL ANEMIA

114
Q

Untreated individuals may give off a musty or mouse- like odor as a side effect of the build-up and excess phenylalanine in the body

A

Classic PKU

114
Q

A stop codon is produced thereby also stopping protein synthesis

A

NONSENSE MUTATION

114
Q

A rare genetic (inherited) condition caused by the mutation in the gene that aids in creating an enzyme known as Phenylalanine Hydroxylase. Due to this mutation, there is a phenylalanine build up in the body.

A

PHENYLKETONURIA

115
Q

Genetic disorder that affects both the lungs and the digestive system.

A

CYSTIC FIBROSIS

115
Q

People with this can develop a very thick and
sticky mucus in their lungs, airways, and digestive system.

A

CYSTIC FIBROSIS

116
Q

Trisomy 21 is the most common type of

A

DOWN SYNDROME

117
Q

an hereditary disorder of the connective tissues which results to abnormally long and thin digits. People with this syndrome may also experience or develop optical and cardiovascular defects

A

MARFAN SYNDROME

118
Q

Genetic condition where the affected person has an extra chromosome which can cause mild to serious physical and developmental problems.

A

DOWN SYNDROME

119
Q

Considered as a rare chromosomal disorder which affects the male population. The affected person has a total of 47 chromosomes.

A

XYY SYNDROME (SUPER MALE)

120
Q

In some cases, affected individuals develop behavioral problems such as an explosive temper, hyperactivity, impulsivity, defiant actions, or, in some cases, antisocial behavior

A

XYY SYNDROME (SUPER MALE)

120
Q

There were many misconceptions about this disease. It was sometimes called the super- male disease
because men with this syndrome were thought to be overly-aggressive and lacking in empathy.

A

XYY SYNDROME (SUPER MALE)

120
Q

Are considered as the MOST ABUNDANT class of bioorganic molecules

A

CARBOHYDRATES

121
Q

monosaccharides containing an aldehyde group

A

ALDOSES

121
Q

Functions:
● Provides energy
● Storehouse of chemical energy
● Supply carbon atoms for the synthesis of other biochemical substances (lipids, nucleic acid,
proteins)

A

CARBOHYDRATES

122
Q

Utilized as a primary source of energy

A

D-GLUCOSE

122
Q

Most important in a human nutritional standpoint

A

D-GLUCOSE

122
Q

monosaccharides containing a ketone group

A

KETOSES

122
Q

A polymeric carbohydrate that
contain a large number of monosaccharide units joined
to the next by one or more
glycosidic bonds

A

POLYSACCHARIDES

122
Q

Dextrose / Blood sugar

A

D-GLUCOSE

123
Q

Contain 2-10 monosaccharide
unit covalently bonded to each
other

A

OLIGOSACCHARIDES

123
Q

bond in a disaccharide resulting from the reaction between the hemiacetal carbon atom -OH group of one monosaccharide and an -OH group on the other monosaccharide

A

GLYCOSIDIC LINKAGE

123
Q

grape sugar

A

D-GLUCOSE

123
Q

Carbohydrates that contain two monosaccharides joined by a glycosidic bond

A

DISACCHARIDES

124
Q

Play an important role in keeping blood glucose concentration within the normal range

A

INSULIN & GLUCAGON

125
Q

● Produced as an intermediate in a hydrolysis reaction
● Contains two D-glucose
monosaccharides
● Cannot be digested by humans or ferment by yeast

A

CELLOBIOSE

125
Q

Low blood sugar level: pancreas secretes

A

GLUCAGON

126
Q

High blood sugar level: pancreas secretes

A

INSULIN

127
Q

Also known as “Malt sugar”

A

MALTOSE

127
Q

Aka “milk sugar”

A

LACTOSE

127
Q

AKA “Brain sugar”

A

D-GALACTOSE

127
Q

Synthesized from glucose in the
mammary glands for use in lactose

A

D-GALACTOSE

127
Q

Present in many fruits and honey

A

D-FRUCTOSE

127
Q

Present as a chemical marker that distinguishes types of blood

A

D-GALACTOSE

127
Q

Most important ketohexose

A

D-FRUCTOSE

127
Q

Aka levulose and fruit sugar

A

D-FRUCTOSE

127
Q

Sweetest-tasting of all sugars

A

D-FRUCTOSE

128
Q

Sometimes used as a dietary sugar

A

D-FRUCTOSE

128
Q

a known component of RNAs and energy-rich compounds such as ATPs

A

D-RIBOSE

128
Q

is classified as a pentose sugar

A

D-RIBOSE

128
Q

Major sugar found in milk

A

LACTOSE

128
Q

Produced whenever the polysaccharide starch breaks down

A

MALTOSE

128
Q

MOST ABUNDANT out of all
disaccharides

A

SUCROSE

128
Q

Important ingredient in commercially produced infant formulas that are designed to stimulate mother’s milk

A

LACTOSE

129
Q

Also known as “common
table sugar”

A

SUCROSE

129
Q

Produced commercially from
juices of sugarcane and sugar
beets

A

SUCROSE

130
Q

These are carbohydrates that contain three to ten (3-10) monosaccharide units that are bonded together by glycosidic linkages

A

OLIGOSACCHARIDES

131
Q

This is a non-reducing sugar

A

SUCROSE

132
Q

● Polysaccharide containing only glucose units
● Form of stored glucose in human and animals

A

GLYCOGEN

133
Q

Known as animal starch

A

GLYCOGEN

134
Q

Ideal storage form for glucose

A

GLYCOGEN

135
Q

Process wherein formation of glycogen occurs

A

Glycogenesis

136
Q

Readily absorbs water, leading to softer stools and
frequent bowel action

A

CELLULOSE

136
Q

Takes place when blood glucose are sufficiently high.

A

Glycogenesis

136
Q
  • Occurs primarily in the liver
  • Stimulated by glucagon and epinephrine
  • Glycogen is broken down into glucose to provide immediate energy and to aid in the maintenance of blood glucose levels during fasting
A

Glycogenolysis

136
Q

Most abundant naturally occurring polysaccharide

A

CELLULOSE

137
Q

● Straight-chain glucose polymer
● Accounts for 15-20% of the starch

A

Amylose

137
Q

Carbohydrate metabolism starts in the

A

MOUTH

137
Q

● Similar to cellulose in both function and structure
● Gives rigidity to the exoskeleton of crabs, lobsters,
shrimps, insects, and other arthropods
● Occurs in the cell wells of fungi

A

CHITIN

137
Q

The major breakdown products of carbohydrate metabolism:

A

Glucose, Fructose, & Galactose

137
Q

PRIMARY SITE for carbohydrate metabolism is the

A

SMALL INTESTINE

137
Q

Desirable intake of dietary fiber

A

25g-35g

137
Q

○ Branched glucose polymer
○ Accounts for 80-85% of
the starch

A

Amylopectin

137
Q

Monosaccharide unit: galactose, glucose, and fructose

A

RAFFINOSE

137
Q

Monosaccharide units: galactose, glucose, fructose,
and an additional galactose

A

STACHYOSE