Chapter 6: Protein Flashcards

1
Q

Amino acid primary sequence

A

determined by the amino acid sequence

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2
Q

Polypeptide shapes- secondary structure

A

-determined by weak electrical attractions with chain
-results in twisting folding of protein
-provides strength and rigidity

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3
Q

polypeptide tangles - tertiary structure

A

-Complex structures
-due to side chain properties (hydrophillic)
-maintaining shape required to function

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4
Q

Multiple polypeptide Interactions

A
  • interactions between polypeptide chains
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5
Q

Protein denaturation

A
  • Disturbs their stability
    -uncoil and lose their shape
    -less functional ability
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6
Q

Causes of Protein Denaturation

A
  • Heat
  • Acid, Base
  • Agitation
  • Alcohol, Heavy Metals
    -other agents
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7
Q

Mouth and Salivary Glands

A

Chewing and crushing moisten protein rich foods and mix them with saliva to be swallowed

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8
Q

Stomach

A

HCl uncoils protein stands and activates stsomach enzymes

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9
Q

Small Intestine and Pancreas

A

Pancreatic and small intestinal enzymes split polypeptides further,
then the enzymes on the surface of the small intestine cells hydrolyze these peptides and the cells absorb them

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10
Q

HCl

A

Denatures protein structure
activates pepsinogen to pepsin

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11
Q

Pepsin

A

Cleaves proteins to smaller polypeptides and some free amino acids
inhibits pepsinogen synthesis

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12
Q

Enteropeptidase

A

Converts pancreatic trypsinogen to trypsin

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13
Q

Trypsin

A

-Ihnhibists trypsinogen synthesis
-cleaves peptide bonds next tothe amino acids lysine and arginine
-converts pancreatic procarboxypeptides to carboxpeptidases
-Converts pancreatic chymotrypsinogen

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14
Q

Chrymotrypsin

A

Cleaves peptide bonds next to the amino acids phonylalnine tryosine, tryptophan, methionine, asparagine and histidines

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15
Q

Protein Absorption

A

Amino acids must transport into intestinal cells
-there are specific carries for amino acids and small peptides

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16
Q

Once amino acids are in intestinal cells

A

Used for energy
synthesis of other compounds
unused proteins are sent to the liver via the bloodstream

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17
Q

Roles of Proteins

A

-Building materials for growth and maintanece
- as enzyme to help facilitate or help a reaction to completion
- As hormones messesnger molecules, released in bloodstream to tissues and elicit appropriate responses

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18
Q

Regulators of fluid balance

A

Proteins attract water
-found in blood and plasma
-do not normally cross cell membranes, when they do this causes problems for the body
-fluid balance like edema

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19
Q

Acid-Base Regulators

A

-acceot and release H+ ions to maintain balance
-disruptions may cause acidosis or alkalosis, resulting in coma or death

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20
Q

As Transporters

A

Found in nlood, cell membranes
-carrt nutrients and other molecules
-act as a pump in cell membrane

21
Q

antibodies

A

invading antigens are destroyed by antibodies
-each antigen = specific antibodies
-molecular memory is called immunity

22
Q

As a source of energy and glucose

A

Proteins can be sacrificed when needed
-body tissues broken down into amino acids
-gluconerogenesis

23
Q

Using amino acids

A

-To make other compounds
-for energy and glucose
-to make fat
- deamination reactions
creates annonia and C structure without amaino group

24
Q

Converting ammonia to urea

A

Ammonia is toxic
-the liver combines ammonia with CO2 to make urea
-Urea is released inti the blood and passes through the kidneys
-direct relationship to dietary protein intake
-water is required

25
Nitrogen balance
nitrogen intake - nitrogen output
26
Conditionally essential amino acids
Tyrosine becomes an essential amino acid if the body doesn't convert phenylanine or if diet it doesn't supply it
27
Protein quality: digestibility
Animal protein- 90-99% soy and legume protein =less than 90% Plant protein 70-90%
28
Amino acid composition
Must get all 9 essential amino acids we do not make partial proteins
29
High quality proteins
animal derived foods and some plant derived foods
30
Complementary proteins A=
Achieved throughout the dayas opposed to each meal
31
measuring protein quality
0-100 100- egg whites, ground beef, chciken, skim milk, tuna
32
Recommendation intakes of protein RDA
0.8 g/kg of healthy body weight increased for various population groups
33
DRI
10-35% daily intake from protein must also ensure consumption of adequate energy daily
34
reasons we need dietary protein
obtain essential amino acids to supply nitrogen to make other proteins
35
Protei Energy undernutrition
insufficient intake of protein, energy or both most commone malnutrition impact on children is poor growth may impact certain adult population
36
Health effects of protein
Heart disease cancer osteoporosis weight control kidney disease
37
protein powders
Commonly whey protein often used post-workout not necessary but can be convenient
38
Amino Acid supplements
Single amino acids do not naturally exist in food s -possibly harmful to the body
39
Difference between proteins and carbs/fats
Nitrogen group that is excreted as urea they are much larger and can fold and configure themselves in unique ways denatured proteins cannot preform functions but can't happen to carbs/fats
40
Protein synthesis
DNA is the templater that determines the amino acid sequence of proteins
41
Translation
the process of mRNA directing the sequence of amino acids and synthesis of protein; the amino acids are collected by tRNA and brought to the ribosomes
42
Transcription
the process of making mRNA from the DNA template
43
Ribosomes
The part of the cell where translation happens and then the completed protein is released
44
DNA
packed with 46 chromosomes segments of DNA are genes genes can be translated into a protein
45
Gene expression
DNA- mRNA- tRNA -Protein genes must be switched on and off
46
single gene disorders
Mutations inherited at birth damage to the individual exerted early in life
47
Multigene disorders
Influence several genes sensitive to interactions with the environment single nucleotide polymorphosis
48
Clinical consideration
-genetic predisposition to specific diseases -personalied therapies based on genetic profile -creation of new medicine for genetic variations -deeper understanding of nutrition and disease pathways -currently look mostly at SNPs