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生卒年月生物化学英文习题讲课讲稿

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2021-01-20 03:51
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兵家思想-生卒年月

2021年1月20日发(作者:minimum)
Chapter1

Nucleic Acids
I

Choose one correct answer. Mark your answer by circling the capital letter you
choose.

1.

The direction of nucleic acid is
A.

From N to C


















B. From 5

to 3


C. From C to N



















D. From 3

to 5


E. None of above
2.

The
description
of
the
secondary
structure
of
DNA
double
helix
are
correct,
EXCEPT

A.

Two antiparallel strands
B.

Deoxyribose-phosphate frame located outside the strands
C.

Two strands are joined by hydrogen bond formed between A-T and G-C
D.

Diameter of helix is 2 nm, and 10 bases in each turn
E.

Nucleosome is the structure unit of DNA double helix
3. The correct description about Tm is

A.

The temperature at which half of the maximum absorbance value of DNA
at 260nm during heat denaturation

B.

The temperature at which maximum absorbance value of DNA at 260nm
during heat denaturation
C.

The optimum temperature for DNA synthesis

D.

High Tm value is related to low G-C content

E.

The temperature to form DNA and RNA hybrid molecule
4.

If the coden of mRNA is ACG
, then the anticoden of tRNA is
A.

UGC



B. TGC




C. GCA



D. CGU



E. TGC
5.

The linkage between nucleotides is


A.

2

,-3

phosphodiester bond;








B.

3

,-5

phosphodiester bond
C.

2

,-5

phosphodiester bond;








D.

Hydrogen bond
E.

Peptide bond
6.

The template strand of D
NA is 5’
-ATTCAG-
3 ’ , its transcript is

A.

5’
-GACTTA-
3’







B.

5’
-CTGAAT-
3’










C.

5’
-UAAGUC-
3’






D.

5’
-CUGAAU-
3’






E.

5’
- TAAGTC-
3’


II

Fill in the blanks.

1.

Eukaryotic
mRNAs
can
be
modified
after
transcription
at
the
5

end
with
a
modified residue called a____________, at the 3

end 80 to 250 A residues are added
to create a ____________.

2.
Each
nucleotide
consists
of
three
components,
_____________,
______________, ______________.
3.

The conformation
for DNA proposed by Watson
and Crick is
called B form,
the other two conformations existing in the cell are ____________, ______________.

III

Explain the following terms.

1.

Hybridization of nucleic acids
2.

Tm
3.

4.

5.

6.

7.

8.

9.

10.


ribozyme
codon
anticodon
Hyperchromic effect
DNA denaturation
Annealing
snmRN
nucleosome
Ⅳ、
Briefly state the following questions.

1. State the functions of three major kinds of RNA (mRNA, tRNA and rRNA).
2. Please describe the secondary structure of DNA proposed by Watson and Crick.
3. State briefly the differences between DNA and RNA.
4. Please describe the structural features of eukaryotic mRNA.

Chapter2

Proteins
I

Choose one correct answer. Mark your answer by circling the capital letter you
choose.

1. All of the following amino acids are acidic or basic amino acids,
EXCEPT


A.

Asp
B.

Glu
C.

Lys
D.

Arg
E.

Ser
2. Which is the linkage bond for the peptide?
A.

Hydrogen bond
B.

Peptide bond
C.

Hydrophobic interactions
D.

Electrostatic interaction
E.

3

, 5



phosphodiester bond
3. The protein molecule (pI=6.5) will mobile the to positive electrode when the pH
of electrophoresis buffer is
A.

pH=3.0
B.

pH=4.0
C.

pH=5.0
D.

pH=6.5
E.

pH=8.0
4. The amino acid in proteins is
A.

L-
β
-aimno acids;

















B.

D-
β
-aimno acids;
C.

L-
α
-aimno acids;

















D.

D-
α
-aimno acids;
E.

All of above
5. The chemical bond in charge of maintaining secondary structure of proteins is
A.

Salt bridge;






















B.

Disulfide bond
C.

Hydrogen bond;


















D.

Peptide bond;
E.

Hydrophobic interaction
6. The chemical bond in charge of the primary structure of proteins is
A.

Salt bridge;






















B.

Disulfide bond
C.

Hydrogen bond;


















D.

Peptide bond;
E.

Phosphodiester bond

II

Fill in the blanks


1.

The
secondary
structures
of
protein
include
___________,
___________,
___________, and ___________.
2.

The
absorbance
peak
value
of
protein
is
at
___________nm,
and
that
of
the
nucleic acid is at ___________nm.

3.
The
force
maintaining
higher
structure
of
proteins
are
noncovalent.
They
are
______________,

______________, _______________, ________________.
III

Explain the following terms.

1.

GSH (glutathione)
2.

Motif
3.

protein denaturation

4.

petptide unit
5.

domain
6.

pI of protein
7.

α
-helix
8.

Peptide bond
9.

amino acid residue

10.

salting out

Ⅳ、
Briefly state the following questions.

1.
List
the
approaches
commonly
used
in
separation
and
purification
of
protein
molecules, and explain simply the major mechanism of each one.
2.
Briefly
explain
the
structural
features
and
classification
of
amino
acids
constitute of different proteins.
3. What is primary structure of protein? Please state the relationships between the
primary structure and functions of proteins by an example.

Chapter3

Vitamins
I

Choose one correct answer. Mark your answer by circling the capital letter you
choose.

1. Vitamin D belongs to
A.

Fat soluble
























B.

Water soluble
C.

Both A and B






















D.

Insoluble
E.

Not above all


2. The active form of Vitamin D is
A.

25-(OH)D
3

























B.

1,25-(OH)
2
D
3

C.

1,24,25-(OH)
3
D
3

D.

24,25-(OH)
2
D
3

E.

Not above all


3. The active form of folic acid is
A.

F
























B.

FH
2

C.

FH
4

D.

NAD
+

E.

FAD
4. The deficiency of which will cause anmia?
A.

Vitamin B
6

























B.

Vitamin B
12

C.

FH
4























D.

All of the above
E.

Not above all

II

Fill in the blanks


1.

____________
and
____________

are
the
cofactors
(coenzymes)
of
the
dehydrogenases,
and
they
are
derived
from
Vitamin
B2;
____________
and
____________
are
also
the
cofactors
(coenzymes)
of
the
dehydrogenases,
and
they
are derived from Vitamin ____________.
2.
The
active
forms
of
vitamin
A
are
____________,
___________and
___________. An early symptom of vitamin A deficiency is ___________

III

Explain the following terms.

1.

provitamin A
2.

lipid-soluble vitamins
3.

water- soluble vitamins

Ⅳ、
Briefly state the following questions.

Try to explain the biochemical functions of vitamin C and its deficiencies.

Chapter4

Enzymes
I

Choose one correct answer. Mark your answer by circling the capital letter you
choose.

1. The factors related to the kinetics of enzyme reaction are included,
EXCEPT

A.

pH and temperature
B.

[Enzyme]
C.

[Substrate]
D.

Inhibitor
E.

Time
2.

About competitive inhibitors, which of the following is
NOT
true?
A.

Similar to the substrates























B.

Bind to the active centre of the enzymes
C.

Bind to the enzyme reversibly.

D.

Bind to the enzyme by non-covalent bond
E.

None of the above


3. About non-competitive inhibitors, which one is true?
A.

K
m

, Vmax
remains constant






















B.

K
m

, Vma
x


C.

K
m


remains constant
, Vmax



D.

K
m

, Vma
x


E.

K
m

, Vmax
remains constant
tion of phosphate pesticide on choline esterase belongs to
A.

Irreversible inhibition
B.

Reversible inhibition
C.

Competitive inhibition
D.

Noncompetitive inhibition
E.

Uncompetitive inhibition

II

Fill in the blanks


1.

The
essential
groups
in
active
center
of
an
enzyme
are
______________and

_________________.



2.

Holoenzyme = _____________ + ____________.
3.

The
three
properties
of
enzymatic
catalyzed
reactions
are
_____________,
______________, _________________.
4. When V equals to 80% Vmax, [S]= ______ Km. When V equals to 90% Vmax,
[S]= ______ Km.
5.
The
specificities
of
enzymes
can
be
briefly
divided
into
three
types:
_____________, ______________and________________.

III

Explain the following terms.

1.

Isoenzyyme
2.

Km
3.

Active center of an enzyme
4.

Allosteric enzyme
5.

Competitive inhibition
6.

Optimum temperature


Ⅳ、
Briefly state the following questions.

1.
What
is
the
activation
of
zymogen?
State
the
biological
significance
of
the
process.
2. Briefly state the significance of
Km
and
Vmax.
3. Compare the characters of three types of reversible inhibition.
Chapter 5

Carbohydrate Metabolism
I


Choose
one
correct
answer.
Mark
your
answer
by
circling
the
capital
letter you choose.

A. pentose phosphate pathway






B. tricarboxylic acid cycle

C.
β
-oxidation of fatty acid









D. glycolysis









E. gluconeogenesis
2. Which compound can
NOT
be used to do gluconeogenesis?
A. Acetoacetate
B. Glycerol
C. Pyruvate



























D. Glutamate
E. Succinate
pathway for mature red blood cells to obtain NADPH is (



)























A. pentose phosphate pathway






B. tricarboxylic acid cycle

C.
β
-oxidation of fatty acid









D. glycolysis




E. gluconeogenesis
4. In the muscle, glucose 6-phosphhate can convert into the following compounds
EXCEPT

A. Glycogen
B. Acetyl CoA
C. Lactate
D. Glucose
E. Fructose 6-phosphate
5. Which compound is
NOT
the coenzyme of pyruvate dehydrogenase complex?
A. FAD
B. NAD
+

C. Biotin
D. CoASH
E. Lipoic acid
6. Which enzyme is the key enzyme in glycogenolysis (glycogen degradation) ?
orylase

nase

oenol pyruvate carboxykinase
-CoA reductase
te kinase


1. The unique pathway for mature red blood cells to obtain ATP is (



)
























II


Fill in the blanks.


1.
The
active
form
of
glucose
in
glycogenesis
is
















,
the
active
form of choline in phospholipid synthesis is

















, the active form of
SO
4
2-

in
sulfation
is










,
the
active
form
of
methyl
in
methylation
is













.
2. Glucose 6- phosphate (G-6-P) is an important intermediate compound involved
in
the
carbohydrate
metabolism
pathways,
e.g.,
____________,
____________,
____________ , ____________, and ____________.

III


Explain the following terms.
1

Glycolysis
2

Tricarboxylic acid cycle
3

Pentose phosphate pathway
4

Glycogenesis
5

Glycogenolysis
6

Gluconeogenesis
7

Blood sugar
8

Cori cycle (Lactate cycle)
9

Glycogenosis or glycogen storage disease
10. Aerobic oxidation

Ⅳ、
Briefly state the following questions.
1. The major function of pentose phosphate pathway.
2. List the major products of Tricarboxylic cycle and pentose phosphate pathways,
and state their biological significance.

3. Simply state the several steps of aerobic oxidation pathway.
4. State the source, fate and regulation of blood glucose.


Chapter 6


Biological Oxidation
I


Choose one correct answer. Mark your answer by circling the capital letter you
choose.


+
?
complex II
?
complex I
?
CoQ
?
complex III
?
cytochrome
1. The order of the members of NADH oxidative respiratory chain is


C
?
complex IV

+
?
complex I
?
complex III
?
CoQ
?
cytochrome C
?
complex
IV

+
?
complex II
?
complex III
?
CoQ
?
complex C
?
complex IV
x II
?
NAD
+
?
CoQ
?
complex III
?
cytochrome C
?
complex
IV

+
?
complex I
?
CoQ
?
complex III
?
cytochrome C
?
complex
IV

+
may be reduced to NADPH in
ysis
eogenesis
e phosphate pathway
pathway of fatty acid degradation
reaction catalyzed by malate dehydrogenase
hydrogen atoms (2H) in cytosolic NADH(+H
+
) are transported from cytosol
to mitochondria through
e
e-pyruvate shuttle
or
?
-glycerol phosphate shuttle
cetate-pyruvate cycle
e phosphate pathway
ons
from
pyruvate
enter
the
mitochondrial
electron
transport
chain
at
the
level of


-CoQ reductase (complex I)
-cytochrome c reductase (complex III)

rome c oxidase (complex IV)


II


Fill in the blanks.
1. The two respiratory chains of oxidative phosphorylation are ____________ and
____________.



2.
Biological
oxidation
is
a
process
in
which
the
____________
are
completely
oxidized
to
____________,
____________

and
a
large
amount
of

____________ released.


III


Explain the following terms.
1.

ATP synthase
2.

Mixed function oxidase
3.

Reactive oxygen species, ROS
4.

?
-Phosphoglycerol shuttle
5.

Malate-aspartate shuttle
6.

Biological oxidation
7.

Oxidative respiratory chain
8.

Oxidative phosphorylation
9.

Free radical
10.

Substrate cycle

Ⅳ、
Briefly state the following questions.

1.
What
is
biological
oxidation?
Compare
the
difference
between
nutrition
oxidation in vivo and nutrition oxidation in vitro.
2.

What is Oxidative phosphorylation? State the order of the members of two
important oxidative respiratory chains.

Chapter 7

Lipid Metabolism
I


Choose
one
correct
answer.
Mark
your
answer
by
circling
the
capital
letter you choose.

A. HMG-CoA synthase
B. Mevalonate kinase
C. HMG-CoA reductase
D. HMG-CoA lyase
E. Squalene epimerase
2. The rate-limiting (key) enzyme for fatty acid synthesis is

A. Acetyl CoA carboxylase
B. Carnitine- acyl transferase
C. Palmitate decarboxylase
D. Acyl CoA transferase

E.
?
-ketoacyl CoA synthetase
3. The precursor for acetoacetate formation in the liver is

1. The rate-limiting (key) enzyme for cholesterol biosynthesis is

A.
?
-hydroxybutyrate
B. Acetoacetyl CoA

C.
?
-hydroxybutyryl CoA
D. Mevalonate

E. HMG-CoA
4. The rate- limiting

key

enzyme for fatty acid synthesis is

A. Acetyl CoA carboxylase
B. Carnitine-acyl transferase
C. Palmitate decarboxylase
D. Acyl CoA transferase

E.
?
-ketoacyl CoA synthetase


5. The oxidation and degradation of fatty acids in the cell







A. Begins with the fatty acid thioester of CoA







B. Does not produce useful energy for the cell







C. Occurs primarily in the nucleus







D. Is inhibited by carnitine







E. Proceeds through successive shortening of fatty acids by three-carbon
units


6. Which of the following
lipases is hormone sensitive?








A. Pancreatic lipase







B. Lipoprotein lipase







C. Liver triacylglycerol lipase







D. Adipose tissue triacylglycerol lipase








E. Phospholipase

II

Fill in the blanks.


1.
One
of
the
common
used
techniques
for
plasma
lipoprotein
classification
is















,
according
to
this
method,
the
lipoproteins
can
be
classified
into










,













,








_____

,












.
initial material for Ketone body synthesis is____________, the key enzyme
is
____________.Ketone
bodies
are
____________,
_____________,and
____________.


II


Explain the following terms.
1. Ketogenesis
2. Depot fat mobilization
3. Lipoprotein
4.
β
-oxidation of fatty acids
5. Ketone bodies
6. LDL
7. Lipid
8. Unsaturated fatty acid
9. Essential fatty acid
10. Hormone-sensitive lipase, HSL

Ⅳ、
Briefly state the following questions.

1. What is the meaning of apolipoprotein, explain their functions.
n the effect of insulin on lipid mobilization.
the classification, the major components, synthesis site of lipoproteins and
their functions
state the regulation functions of insulin on lipid metabolism.

Chapter 8

Protein Catabolism
I


Choose
one
correct
answer.
Mark
your
answer
by
circling
the
capital
letter you choose.

A. to replenish ribose 5-phosphate
B. as an initial material for synthesizing pyrimidine
C. to provide active sulfate group for sulfation of some compounds
D.

to provide methyl group for methylation of some compounds
E.

an enzyme involved in biosynthesis of cholesterol
important role of S-adenosylmethionine is

A. to replenish methionine
B.

to synthesize tetrahydrofolic acid
C.

to provide methyl group for methylaton
D.

to produce adenosine
E.

to synthesize homocysteine
3.

Which of the following amino acids is nutritionally non- essential amino acid?
A. Phenylalanine
B. Glutamate

C. Methionine
D. Tryptophan
1. The important role of PAPS is

E. Threonine
4. Which amino acid is nutritionally essential?

A. Aspartate









B. Glutamic acid










C. Alanine


D. Tyrosine










E. Methionine
5. The transportation form of ammonia in blood is

A. Glutamate
B. Tyrosine
C. Glutamine
D. Glutathionine
E. Aspartate
6. One carbon units produced in amino acid metabolism are included,
EXCEPT

A. CH
3
-
B. CH
2
-
C. O=CH-
=CH-
E. CO
2

II


Fill in the blanks.
1.

























is the active form of methionine for providing


methyl group to methylation of many biological molecules.

2.



























is the active form of sulfate for adding sulfate
group to sulfation many biological molecules.
3.
The
transamination
reactions
of
amino
acid
are
____________,
_______________ , and_______________.

The major transaminase in the heart
is _______________, and in the liver is ____________.

III


Explain the following terms.



1. Nitrogen balance
cycle (Ornithine cycle)
carbon unit
mination
ed deamination
ial amino acid
action
enic amino acids
methionine
10. Pyridoxal phosphate

Ⅳ、
Briefly state the following questions.

1. The major process of urea synthesis.
2. State the source and fate of amino acid in vivo.
3. State protein putrefaction and the important products of putrefaction.




Chapter 9

Nucleotide metabolism
I


Choose
one
correct
answer.
Mark
your
answer
by
circling
the
capital
letter you choose.

nuecleotides is


1

The first synthesized purine nucleotide in the de novo synthesis of purine



A. AMP













B. GMP

















C. CMP
D. IMP














E. UMP
2. One of the properties in purine de novo synthesis is that

A. the first step is the production of PRPP
carbon unit is provided by S-adenosylmethionine
e phosphate is an intermediate
e does not incorporate in the pathway
E. aspartate is the direct nitrogen donor
end catabolic product of purine nucleotides in human is

A. Urea










B. Uric acid








C. Creatinine
D. Creatine







E.
?
-alanine
of the properties in pyrimidine synthesis is that (



)
base is synthesized based on 5-phosphoribose
carbon unit is provided by FH
4

glycine molecule incorporates in the synthesis
first synthesized intermediate is carbamoyl phosphate
ate is the nitrogen donor
is the end product of purine degradation in humans?







A.

NH3

B. CO
2

C. Uric acid

兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月


兵家思想-生卒年月



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