Amino Acids & Protein Flashcards

1
Q

are the building blocks of proteins

A

amino acids

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2
Q

amino acids have __ a code in your amino group, it also has ___ group

A

N terminal, carboxyl group

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3
Q

differs in every amino acids, determines the chemical behavior of that particular amino acid

A

side chain

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4
Q

10 essential amino acids

A

arginine
histidine
isoleucine
leucine
lysine
methionine
phenylalanine
threonine
typhthopan
valine

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5
Q

amino acids with positively charged side chain

A

arginine, histidine, lysine

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6
Q

amino acids with negatively charged side chain

A

aspartic acid, glutamic acid

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7
Q

amino acids with uncharged side chains

A

serine, threonine, asparagine, glutamine

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8
Q

special cases amino acids

A

cysteine, selenocysteine, glycine, proline

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9
Q

amino acid with hydrophobic side chains

A

alanine
isoleucine
leucine
methionine
phenylalanine
tryptophan
tyrosine
valine

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10
Q

protein forming from amino acids starts with

A

a cell

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11
Q

the nucleus contains the ___, it is then split into ___ pairs of chromosome

A

genome, 23 pairs of

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12
Q

each chromosome contains a long strand of __, they are tightly packed around histones

A

DNA

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13
Q

within the DNA are sections called ___ they contain instructions for making proteins

A

genes

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14
Q

when the genes are switched on, an enzyme called ____ attaches to the gene

A

RNA polymerase

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15
Q

RNA polymerase attaches to the gene, it moves along the DNA making a strand of RNA out of 3 bases in the nucleus, the code then determines the order in which the bases are added to the mRNA.

A

transcription

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16
Q

before the mRNA can be used as a template for the production of proteins, it needs to be processed. this involves

A

removing and adding sections of RNA

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17
Q

moves out of the nucleus into the cytoplasm

A

messenger RNA

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18
Q

protein factories in the cytoplasm , binds to the mRNA

A

ribosomes

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19
Q

reads the code in the mRNA to produce a chain made up of amino acids

A

ribosome

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20
Q

there are ___ types of amino acids

A

20 types of

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21
Q

carries the amino acids to the ribosome

A

tRNA

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22
Q

mRNA reads ___ bases at a time

A

3 bases

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23
Q

as each triplets are read ___ delivers the corresponding amino acids, which is added to a growing chain of amino acid

A

tRNA

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24
Q

once the last amino acid has been added, the chain folds into a complex 3D shape to form the?

A

protein

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25
amino acids are linked by a ___ thats why proteins are ____
peptide bond, polypeptide
26
polypeptide will fold based on the confirmation depending on the interaction between the
amino acid side chain
27
macromolecules made up of amino acids
protein
28
most of your proteins are synthesized in the
liver
29
immunoglobulins are synthesized in the
plasma cells
30
only contains amino acids and peptide bonds
simple proteins
31
combination of amino acids plus non protein group
conjugated proteins
32
carry lipid (carriers) considered as conjugated because it has amino acid but also contain a non protein
lipoprotein
33
diff shapes of protein
fibrous, globular, simple globular
34
fibrous proteins
fibrinogen, streponins, collagen
35
globular proteins
hgb, plasma, proteins, enzymes, peptide hormones
36
are compact, meaning they have little or no space for water in that molecule
simple globular proteins
37
tissue nutrition
energy
38
maintenance of water distribution between cells and tissue, interstitial compartments, and the vascular system of the body
osmotic force
39
participation as buffers to maintain pH
acid base balance
40
metabolic substances
transport
41
part of immune defense system
antibodies
42
hormones and receptors
hormones
43
connective tissue
structure
44
catalysts
enzymes
45
participation in coagulation of blood
hemostasis
46
basis of folding will depend on the side chain of the amino acids which is your
R
47
4 structures of protein
primary, secondary, tertiary, quarternary structure
48
linear sequence of amino acids, but this structure can already determine the identity of protein, the molecular structure, the binding capacity and recognition ability
primary structure
49
a repeating structure. it involves the winding of your polypeptide chain. it can form sheets which are called **beta pleated sheets** it could also curl which is called an **alpha helix**
secondary structure
50
it can add strength and flexibility to your protein
secondary structure
51
there is a 3D configuration, there is a folding pattern of your protein, this is responsible for the many chemical and physical properties of your protein
tertiary structure
52
functions of protein
energy, osmotic pressure, acid base balance, transport, antibodies, hormones, structure, enzymes, hematosis
53
secondary structure can form sheets which are called
beta pleated sheets
54
secondary structure can also curl which is called an
alpha helix
55
there are associations of 2 or more polypeptide chains. this forms a functional protein molecule
quarternary structure
56
can determine the identity, molecular structure, binding capacity and recognition ability
primary structure
57
responsible for the many chemical and physical properties of protein
tertiary structure
58
a principal fetal protein which is used to assess maternal serum as screening test for any fetal conditions
alpha fetoprotein
59
has the highest concentration of plasma
albumin
60
if we test for proteins we test
total protein - albumin = globulins
61
indicator of nutrition, binds thyroid hormones and retinol binding protein
prealbumin
62
binds bilirubin, steroids, fatty acids, major contributor to oncotic pressure
albumin
63
acute phase reactant, protease inhibitor
alpha 1 antitrypsin
64
elevated levels of alpha fetoprotein indicates risk for
spina bifida
65
acute phase reactant, may be related to immune response
alpha 1 acid glycoprotein (orosomucoid)
66
transport lipids (HDL)
alpha 1-lipoprotein
67
inhibits serine proteinases
alpha 1 antichymotrypsin
68
component of leukocyte antigen (HLA) molecules
B2-microglobulin
69
immune responses
c1q, c3, c4 complement
70
precursor of fibrin clot
fibrinogen
71
acute phase reactant, motivates phagocytosis in inflammatory disease
C-reactive protein (CRP)
72
antibodies
immunoglobulin G, A, M, E, D
73
antibodies in secretions
immunoglobulin A
74
antibodies in early response
immunoglobulin M
75
antibodies in reagins and allergy
immunoglobulin E
76
transports iron
transferrin
77
binds heme
hemopexin
78
most common acute phase reactant, oxidase activity, contains copper
ceruloplasmin
79
ceruloplasmin is also a marker for
wilson’s disease
80
LDL is a?
beta globulin
81
rough measure of all the proteins in the plasma
total proteins
82
total protein low result
hypoproteinemia
83
states that there is a negative nitrogen balance, there is more catabolism breakdown and there is combination or growth than anabolism
hypoproteinemia
84
high total protein
hyperproteinemia
85
a result of dehydration or excessive production of protein
hyperproteinemia
86
clinical adult range of total protein
6.5-8.3 g/dL
87
is not a part of routine examination
protein examination
88
is a big NO because it may falsely elevate the total protein
hemolyzed sample
89
is preferred rather than plasma, because anticoagulant slowly dilutes the proteins in the plasma
serum