Biochemistry WGU OA 2022 Questions With
Answers
Amino Acid backbone consists of Ans - 1. amino group
2. carboxyl group
3. alpha carbon
4. R group
Amino group: looks likes/consists of Ans - NH3+
Carboxyl group looks like/consists of Ans - coo-
Alpha carbon looks like/consists of Ans - CH
The three Amino acid categories Ans - 1. hydrophobic (nonpolar)
2. polar
3. charged
Hydrophobic Amino Acids Ans - non polar
afraid of h20
usually in the middle/core of the protein
contains H + C... C-C, or C-H
Polar Amino Acids Ans - ELECTRONEGATIVE
contains O + H... O-H. NH, SH
Charged Amino Acids Ans - either negative or positive Ionic
Amino Acid Protein structure levels Ans - 1. primary
2. secondary
3. tertiary
4. quaternary
what level do all proteins have Ans - tertiary
Primary level of protein/amino acid Ans - held together with peptide
bonds.
peptide bonds hold amino acids together which forms polypeptide chains
when multiple amino acids are attached together
Secondary Level of protein/Amino acid Ans - forms hydrogen bonds with
the amino back bone
,Tertiary Level of protein/amino acid Ans - The R groups interact to
create the three dimensional shape
Quaternary Level of protein/amino acid Ans - two or more subunits . Not
all proteins have a quaternary structure.. this is where multiple amino acids
are attached by polypeptide chains
hydrophobic interactions Ans - weak. Can be broken with change in
temp. (increasing temp)
if in the center of the protein, they are stronger
aggregation Ans - occurs due to hydrophobic interactions..
when hydrophobic interaction is broken, they bind to other hydrophobic
amino acids.
(boiling an egg)
Hydrogen bonds Ans - bond with O or N
weak. but the more bonds formed the more strength there is.
broke by increased temp and change in PH
disulfide bond Ans - covalent bond. two sulfur atoms
only cysteine forms this bond.
very strong. not easily broken
only broken by reducing agents
Ionic bond Ans - occur by opposite charges
+ attracts -
moderately strong.
broken by change in ph, or salt. increased salt competes with the ionic bond.
enzymes Ans - protein catalyst that help protein reactions happen
quickly.
binds to active site
active site Ans - where the substrate binds. forming a complex.
(enzyme molecule complex)
activation energy Ans - lowers the amount of energy needed to get the
product.
catalyzed reaction
enzyme catalyzed reaction Ans - activation energy is less for the
catalyzed reaction
enzyme Ans - ends in ASE
, substrate Ans - is always before the arrow of the reaction. they can
become products
affinity Ans - an attraction to
myoglobin Ans - higher affinity than hemoglobin.
job is to store o2
has one subunit which binds to one heme group o2 and that o2 has one iron
hemoglobin Ans - picks up o2 from lungs and delivers to tissues
has four subunits (proteins) and each one binds to one heme group o2 and
each o2 has one iron
cooperatively
which class of amino acids is most likely to be located on the exterior of
hemoglobin. why Ans - Polar or charged.
sickle cell anemia results when someone inherits 2 mutant copies of the HBB
gene, which is on chromosome 11. what is the mode of inheritance. Ans -
autosomal recessive
autosomal recessive Ans - you have to get 2 mutated genes to have the
disease
autosomal dominant Ans - you can get only one mutated gene and still
have the disease
in the lung what do we want hgb to do Ans - pick up o2.
relaxed state
high ph: low co2. low H+
high affinity
in the muscle what do we want hgb to do Ans - drop off o2.
low affinity .
tense state
low ph: high co2, high H+
hemoglobin: oxygenated location Ans - lungs
stabilized by co2
Hemoglobin DeOxygenated location Ans - muscle
stabilized by 2,3-BPG
Bohr effect Ans - higher ph has higher % hgb saturated
(higher affinity the higher the ph)
shift to the left is a higher affinity and a shift to the right is a lower affinity
Answers
Amino Acid backbone consists of Ans - 1. amino group
2. carboxyl group
3. alpha carbon
4. R group
Amino group: looks likes/consists of Ans - NH3+
Carboxyl group looks like/consists of Ans - coo-
Alpha carbon looks like/consists of Ans - CH
The three Amino acid categories Ans - 1. hydrophobic (nonpolar)
2. polar
3. charged
Hydrophobic Amino Acids Ans - non polar
afraid of h20
usually in the middle/core of the protein
contains H + C... C-C, or C-H
Polar Amino Acids Ans - ELECTRONEGATIVE
contains O + H... O-H. NH, SH
Charged Amino Acids Ans - either negative or positive Ionic
Amino Acid Protein structure levels Ans - 1. primary
2. secondary
3. tertiary
4. quaternary
what level do all proteins have Ans - tertiary
Primary level of protein/amino acid Ans - held together with peptide
bonds.
peptide bonds hold amino acids together which forms polypeptide chains
when multiple amino acids are attached together
Secondary Level of protein/Amino acid Ans - forms hydrogen bonds with
the amino back bone
,Tertiary Level of protein/amino acid Ans - The R groups interact to
create the three dimensional shape
Quaternary Level of protein/amino acid Ans - two or more subunits . Not
all proteins have a quaternary structure.. this is where multiple amino acids
are attached by polypeptide chains
hydrophobic interactions Ans - weak. Can be broken with change in
temp. (increasing temp)
if in the center of the protein, they are stronger
aggregation Ans - occurs due to hydrophobic interactions..
when hydrophobic interaction is broken, they bind to other hydrophobic
amino acids.
(boiling an egg)
Hydrogen bonds Ans - bond with O or N
weak. but the more bonds formed the more strength there is.
broke by increased temp and change in PH
disulfide bond Ans - covalent bond. two sulfur atoms
only cysteine forms this bond.
very strong. not easily broken
only broken by reducing agents
Ionic bond Ans - occur by opposite charges
+ attracts -
moderately strong.
broken by change in ph, or salt. increased salt competes with the ionic bond.
enzymes Ans - protein catalyst that help protein reactions happen
quickly.
binds to active site
active site Ans - where the substrate binds. forming a complex.
(enzyme molecule complex)
activation energy Ans - lowers the amount of energy needed to get the
product.
catalyzed reaction
enzyme catalyzed reaction Ans - activation energy is less for the
catalyzed reaction
enzyme Ans - ends in ASE
, substrate Ans - is always before the arrow of the reaction. they can
become products
affinity Ans - an attraction to
myoglobin Ans - higher affinity than hemoglobin.
job is to store o2
has one subunit which binds to one heme group o2 and that o2 has one iron
hemoglobin Ans - picks up o2 from lungs and delivers to tissues
has four subunits (proteins) and each one binds to one heme group o2 and
each o2 has one iron
cooperatively
which class of amino acids is most likely to be located on the exterior of
hemoglobin. why Ans - Polar or charged.
sickle cell anemia results when someone inherits 2 mutant copies of the HBB
gene, which is on chromosome 11. what is the mode of inheritance. Ans -
autosomal recessive
autosomal recessive Ans - you have to get 2 mutated genes to have the
disease
autosomal dominant Ans - you can get only one mutated gene and still
have the disease
in the lung what do we want hgb to do Ans - pick up o2.
relaxed state
high ph: low co2. low H+
high affinity
in the muscle what do we want hgb to do Ans - drop off o2.
low affinity .
tense state
low ph: high co2, high H+
hemoglobin: oxygenated location Ans - lungs
stabilized by co2
Hemoglobin DeOxygenated location Ans - muscle
stabilized by 2,3-BPG
Bohr effect Ans - higher ph has higher % hgb saturated
(higher affinity the higher the ph)
shift to the left is a higher affinity and a shift to the right is a lower affinity
