Protein Flashcards

1
Q

9 essential amino acids

A
histadine
isoleucine
leucine
lysine
methionine
valine
phenylalanine
threonine
tryptophan
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2
Q

5 non-essential amino acids

A
alanine
aspartic acid
glutamic acid
serine
asparginine
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3
Q

6 conditionally essential amino acids

A
arginine
cysteine
glutamine
glycine
proline
tyrosine
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4
Q

protein chains of AAs joined together called

A

peptides

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5
Q

what kind of reaction forms peptides

A

condensation reaction

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6
Q

what bonds join amino acids

A

peptide bonds

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7
Q

2 AAs joined by peptide bond called

A

dipeptide

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8
Q

aspartic acid bonded to phenylalanine forms a dipeptide known as

A

aspartame

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9
Q

3 AAs joined by peptide bond called

A

tripeptides

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10
Q

L-cysteine, L-glutamate & glycine form a tripeptide called

A

glutathione

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11
Q

can amino acids act as buffers

A

yes

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12
Q

what is denaturing

A

unfolding proteins by breaking the peptide bonds - makes them unable to function

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13
Q

ex of denaturing agents

A
heat
organic solvents
mechanical mixing
strong acids or bases
detergents
heavy metals
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14
Q

ex of a denatured protein

A

cooked egg white

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15
Q

gene mutation causes protein misfolding causes

A

disease

eg - amyloid protein in alzheimers

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16
Q

Functions of proteins

A
structure of body tissues - collagen
movement - actin & myosin fibres
carrier molecules - haemoglobin
storage molecules - ferritin
fluid balance in blood - albumin
enzymes
hormones - insulin
immune function - antibodies
clotting mechanisms
alternative energy source (carb more efficient)
control of gene expression
cell membrane receptors
17
Q

building blocks of protein

A

amino acids

18
Q

describe protein digestion

A

HCL in stomach converts pepsinogen > pepsin, protein chains broken down into polypeptides
small intestine cck & secretin released, stimulates pancreatic juices
trypsin & chymotrypsin continue chopping up polypeptides
peptidases in small intestine break down further
amino acids & small peptides absorbed into bood