AA and proteins -W1 Flashcards by Dasha shvili

What elements make up carbohydrates

C H O

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What elements make up lipids

C H O

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What elements make up proteins

C H O N

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Primary macronutrients

Carbs
Protein
Fats
Water

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What are macronutrients and primary functions

Needed in larger amounts to support normal function

Provide energy 
Growth
Maintenance 
Support/structure 
Regulate body processes

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Primary micronutrients

Vitamins

Minerals

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What are micronutrients and primary function

Required in smaller amounts 
key roles in metabolism 
Structure 
Growth 
Maintenance 
Regulation

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How many types of amino acids are there

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Structure of amino acid

Amino end (NH2)
Carboxyl end (C=O, OH)
R group

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What does the property of an amino acid depend on

R side chain

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Properties of R side chain on AA and subsequent location

Charged, polar, hydrophilic - usually exposed on surface

Non polar
Hydrophobic - buried in hydrophobic interior or fire of proteins

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AA used for…

Building proteins
Energy production
Converted to glucose
Precursors for: hormones, neurotransmitters, melanin

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In a protein AA are held together by what type of bond

How is this bond made

Peptide bond

Dehydration synthesis

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What determines the primary structure if a protein

DNA

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What determines secondary and tertiary protein structures and functions

Primary structure

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What bonds form secondary protein structures

Between what

H bonds
Between
H of amino group
O of carboxyl group

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What are the two types of secondary protein structures

Alpha helices

Beta pleated sheets

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In alpha helices

The backbone is more stable in a ………… helix

Right handed (clockwise)

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What bonds are formed in formation of tertiary structures

Between what

Hydrogen 
Ionic 
Van der walls forces 
Hydrophobic interactions 
Disguise bonds

Between AA R-group side chains

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What bonds are present in quaternary structures

Weak interactions

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Two types of protein classification

Globular

Structural

Structural proteins (fibrous) 
characteristics 
Use

Insoluble
Low turnover

Ideal for mechanical support and strength

Globular proteins (functional)
characteristics

Compact 
Spherical 
Soluble 
Chemically active 
High turnover

Structural proteins example

Collagen
Keratin
Elastin

Globular proteins example

Enzymes Hormones Antibodies Receptors

Where is haemoglobin found

RBC

Haemoglobin main function

Oxygen transport

Haemoglobin composition

4 polypeptide chains (globin) | 4 non-protein haem groups

What can happen if haemoglobin if folded incorrectly

Sickle cell anaemia

Collagen makes up .......% of protein in the body

25%

How is collagen dispersed until he body

As gel | Or tightly bundled

Collagen: what could go wrong

Osteogenesis imperfecta (Brittle bone disease) Scurvy

Osteogenesis imperfecta | Brittle bone disease

Collagen formation- Glycine replaced by by other AA with bulky side chain Prevents formation of triple helix structure Bones easily fracture Poor wound healing

Scurvy

Collagen formation Caused by lack of Vitamin C (involved in forming cross links between triple helices -making collagen fibril) Decreases tensile strength Causes brushing teeth fallout bleeding gums

'Denatured' protein , ie......

Disruption of interactions/bonds of secondary, tertiary, quartenary structures - -> unfolding - -> loss of function

What causes denatured proteins

pH Temperature Solvents Chemical modification

Denatured proteins- pH

Acids and bases disrupt ionic charge between SIDE CHAINS Eg Protein digestion in stomach

Denatured proteins- temperature

Heat --> energy --> breaking bonds Causing unfolding Eg Sterilising medical instruments with heat to denatured proteins in bacteria

Denatured proteins- solvents

Disrupts SIDE CHAIN bonding Eg Alcohol disinfectant Penetrates bacteria cell wall and denatured proteins and enzymes

Denatured proteins- chemical modification

Eg Oxidation Glycosylation

1g protein = ?? Cal

4.2

Conversion factor from cal --> kj

~ x4

Protein | Recommended dietary intake

0.8g/kg of body weight

Protein is .......% of total energy intake

15-25

Dietary protein- animal products

Meat Dairy Eggs

Dietary protein- plant products

Soy Legumes Whole grains Nuts

How many essential AA

A deficiency in just 1 AA can result in

Decreased protein synthesis

Benefits / negatives of animals as a source of protein

Have similar AA profile to humans higher levels of sat fats lower in fibre Less micronurients

Benefits and negatives (exception) of plants as a source of protein

More fibre and micronutrients Need to eat more and a larger variety to get all amino acids - can have low levels of one or more AA (different chem profile) Exception = soybeans