PCP 2 Flashcards
Chemical elements that form most of living biological matter
CHON
BIOMOLECULES
What are the monomers of:
- carbohydrate
- protein
- lipid
- nucleic acid
- monosaccharide
- amino acid
- glycerol & fatty acids
- nucleotide
What are the elements comprising
- carbohydrate
- protein
- lipid
- nucleic acid
- CHO
- CHONPS
- CHO
- CHONP
Function of carbohydrate
body’s primary source of energy
ex. starch, cellulose, sugars
Function of protein
for growth and repair
ex. muscle, hair, nails, enzymes
Function of lipids
long-term energy storage, insulation, hormones, cell membrane
ex. oil, wax, fat
Function of nucleic acid
genetic information storage, protein synthesis
ex. DNA, RNA
3 Examples of Disaccharides
- saccharose
- lactose
- maltose
3 Examples of Assimilable Polysaccharides
- starch
- amylose
- amylopectin
Glucose + Fructose
Sucrose
Galactose + Glucose
Lactose
2 Glucose
Maltose
(CH2O)n is a formula for what macromolecule
carbohydrates
Which macromolecule does not dissolve in water?
lipids
Monosaccharides have yellow appearance and are soluble in water. True or False?
False, they are colorless and are soluble in water
C10 to C20 natural fatty acids
capric, lauric, myristic, palmitic, stearic and arachidic
Lipids are used by the body to perform all of the following functions EXCEPT:
A. membrane structural material.
B. enzyme action.
C. insulation.
D. a rich energy source.
B. enzyme action.
2 Polyunsaturated fats
Omega-3s & Omega-6s
2 Types of Trans fats
Conjugated linoleic acids (natural)
Partially hydrogenated oils (artificial)
Fats that have fatty acids with only single covalent bonds in their carbon skeletons are
saturated
Accounts for 95% of the fat in our diet and formed with the combination of glycerol and 3 fatty acids
triglycerides
Contain no C-C double bonds
saturated fats
Contain 1 C-C double bond
monounsaturated fats
Contain 2 or more C-C double bonds
polyunsaturated fats
Contain C-C double bonds in a trans rather than cis configuration
trans fats
Which has the higher melting point:(a) a triglyceride containing only lauric acid and glycerol or (b) a triglyceride containing only stearic acid and glycerol?
(b) a triglyceride containing only stearic acid and glycerol
which is a polymer?
- nucleic acid
- fatty acid
- amino acid
- glycerol
nucleic acid
Nucleic acids of DNA only
- thymine (N)
- 2-deoxyribose (S&P)
Nucleic acids of RNA only
- uracil (N)
- ribose (S&P)
Nucleic acids of DNA & RNA
- adenine, guanine, cytosine (N)
- phosphate (S&P)
What are described as the “building blocks of Protein”?
amino acids
Proteins are _____ made of amino acid______.
polymers; monomers
In this type of structure, most of carbonyl groups of peptide bonds forms a hydrogen bond with the amide nitrogen of another peptide bond four amino acids further down the polypeptide chain:
alpha-helix
The isoelectric point of an amino acid is defined as the pH
where the molecule carries no electric charge
The term “SALTING IN” refers to?
Increasing the solubility of a protein in solution by adding ions.
Salting Out
proteins become less soluble at high salt concentrations
The local spatial arrangement of a polypeptide’s backbone atoms without regard to the conformation of its side chains can be called as
secondary structure
The primary stabilizing force of protein secondary structure is
hydrogen bonds
Two types of -pleated sheets can be called:
parallel and antiparallel
Which of the following is NOT a characteristic of a globular protein?
Polypeptide chain in extended, long
sheets
Some parts of a protein that have a specific chemical structure and function are called protein
domains
One of the following is NOT usually a force that helps to hold the monomer units of a quaternary protein together?
A. Peptide bonds
B. Disulfide bonds
C. Salt bonds
D. Hydrophobic interactions
A. Peptide bonds
Which of the following is a secondary structure breaker/alpha helix terminator?
Pro (Proline)
The quaternary structure of a protein is
the intertwining of two or more polypeptides
The action of disrupting the three- dimensional shape of a protein is termed
denaturation
The amino acid found in protein structure
Arginine
The bonds in protein structure that are not broken on denaturation
Peptide bonds
What is the product of the oxidation of dopamine
Reverse reaction occurs via methylation
R-Epinephrine
A heterocyclic aromatic compound consisting of pyrimidine ring fused to an imidazole ring
Purine (Adenine, Guanine)
A heterocyclic aromatic compound similar to benzene and pyridine, containing 2 N atoms at positions 1,3.
Pyrimidine (Cytosine, Uracil, Thymine)
What is the role of hydrogen bonds in the structure if DNA?
to connect the base pairs
Nucleoside is a pyrimidine or purine base
covalently bonded to a
sugar
In gel electrophoresis, what fragments will move most quickly through a gel?
small fragments
Nucleotide bases and aromatic amino acids absorb light respectively at
260 & 280 nm
Which is true about the pairing of bases in the DNA molecule?
purines always pair with
pyrimidines
Enzymes have names that
can end either in -in or -ase
The protein portion of a conjugated enzyme is called a(n)
protein portion of the enzyme without the cofactors
apoenzyme
Enzyme cofactors that bind covalently at the active site of an enzyme are referred to as
prosthetic groups
An enzyme active site is the location in an enzyme where substrate
molecules
undergo change
What is the optimal temperature range for the majority of enzymes?
35-40 C
An allosteric activator
- increases the binding affinity
- stabilizes the R state of the protein
The location on an enzyme where binding occurs is known as the
active site
NAD+, FAD, and FMN are all cofactors for
Oxidoreductases
Allosteric activator
- speeds up reaction
- maintain Vmax
Which of the following kinetic parameters best describes how well suited a specific compound functions as a substrate for a particular enzyme?
kcat/Km => catalytic efficiency
The rate-determining step of Michaelis Menten kinetics is
the complex dissociation step to produce product
Competitive vs Non-competitive inhibitor
C: Vmax same, Km increases
NC: Km same, Vmax decreases
Which of the following binds to an enzyme at its active site?
reversible competitive inhibitor
An uncompetitive inhibitor binds to ____.
ES
A reversible inhibitor that can bind to either E alone or the ES complex
is referred to as a ______
non-competitive inhibitor
A competitive inhibitor of an enzyme is usually
structurally similar to the substrate
In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?
It changes the x-intercept
Glycolytic pathway regulation involves
feedback, or product, inhibition by ATP
The released energy obtained by oxidation of glucose is stored as
ATP
The enzymes of glycolysis in a eukaryotic cell are located in the
cytosol
ATP is from which general category of molecules?
Nucleotides
Where does glycolysis occur?
cytoplasm
Sports physiologists wanted to monitor athletes to determine at what point their muscles were functioning anaerobically. They could do this by checking for a buildup of which of the following compounds?
lactate
Coenzyme Q is involved in electron transport as
a lipid-soluble electron carrier
During glycolysis, electrons removed from glucose are passed to
NAD+
FAD is reduced to FADH2 during
Krebs cycle
Almost all of the oxygen (O2) one consumes in breathing is converted to:
water
The carbon dioxide is primary a product of
krebs cycle
Cellular respiration takes place mostly in:
mitochondria
Which of the following is not present during the TCA cycle?
O2
Which of the following is an aerobic product of pyruvate catabolic metabolism?
ethanol
The Krebs Cycle begins when pyruvic acid produced by glycolsis enters the
mitochondrion
The main purpose of the electron transport chain is to:
Use high energy electrons from other cycles to convert ADP into ATP
Where are the proteins of the electron transport chain located?
mitochondrial inner membrane
The ATP synthase responsible for most of the ATP synthesis in the body is located:
On the inner side of the inner mitochondria membrane
Hydrolysis of a triglyceride produces
fatty acids and glycerol
The site of amino acid catabolism is the:
liver
The first step in the catabolism of most amino acids is
Removal of the amino group
A glucogenic amino acid is one which is degraded to
pyruvate or citric acid cycle intermediates
Transamination is the process where
α-amino group is removed from the amino acid to a keto acid
Both strands of DNA serve as templates concurrently in
replication
Which of the following repairs nicked DNA by forming a phosphodiester bond between adjacent nucleotides?
DNA ligase
During which of the following process a new copy of a DNA molecule is precisely synthesized?
replication
Which of the following enzyme adds complementary bases during replication?
polymerase
Which of the following enzymes unwind short stretches of DNA helix immediately ahead of a replication fork?
helicases
Which DNA polymerase removes RNA primers in DNA synthesis?
Polymerase I
Enzyme, responsible for proofreading base pairing is
DNA Polymerase
The synthesis of DNA by DNA polymerase occurs in the
5’ to 3’ direction
The 5’ and 3’ numbers are related to the
carbon number in sugar
Which of the following enzyme is used for synthesis of RNA under the direction of DNA?
RNA polymerase
Recognition/binding site of RNA polymerase is called
promoter
The site of protein synthesis is
ribosome
The structure in a bacterium that indicates an active site for protein synthesis is
a polysome.
During the process of translation
the peptide is ‘passed’ from the tRNA in the P-site to the tRNA in the A-site
The nucleolus of the nucleus is the site where:
rRNA is transcribed and ribosomal subunits are assembled
The ribosomes are composed of
proteins and RNA
In the genetic code there are:
more codons than amino acids
the anticodon of tRNA
binds to an mRNA codon
On the ribosome, mRNA binds
to the small subunit
Ribosomes select the correct tRNAs
solely on the basis of their anticodons
Which of the following amino acid starts all proteins synthesis?
Methionine
