Lecture 2 Outline Flashcards

1
Q

What are the properties of molecules that are essential for life?

A
  1. Carbohydrates
  2. Nucleotides, Nucleosides & Nucleic acids
  3. Lipids
  4. Proteins
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2
Q

How are proteins molecular tools?

A

Proteins are the tools of cells:

  • proteins are versatile, & carry out many different jobs
  • in any given mammalian cell, there are 10 000-15 000 different types of proteins expressed!

Fibrous vs globular proteins

  • fibrous proteins are generally insoluble
  • globular are usually soluble (functionally, there are 7 categories of soluble protein)
    1. enzymes
    2. membrane transporters
    3. signal molecules
    4. receptors
    5. binding proteins
    6. regulatory proteins
    7. immunoglobulins
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3
Q

Definition of Biomolecules

A

organic molecule that is commonly associated with life (carbohydrates, lipids, nucleic acids, & proteins)

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4
Q

What are examples of Nucleic acids?

A
  • ATP
  • adenosine
  • GTP
  • guanosine
  • cAMP
  • cGMP
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5
Q

What are the carbohydrates properties?

A
  1. general formular of CnH2nOn
  2. most are hydrophilic (“like” water, water soluble)
  3. very abundant in nature
  4. used for structure & energy
    - almost all eukaryotic cells can use glucose for energy & can store some form of glucose (monomer or polymer) for energy
    - many proteins & lipids are modified by the addition of carbohydrates
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6
Q

List & define the 3 groups of Carbohydrates

A
  1. Monosaccharides - are simple sugars
    - most common monosaccharides are the builiding blocks of complex carbohydrates & have either 5 carbons, like ribose, or 6 carbons, like glucose
  2. Disaccharides - consist of glucose plus another monosaccharide
  3. Polysaccharides - are glucose polymers
    - all living cells store glucose for energy in the form of a polysaccharide
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7
Q

What are the lipids properties?

A

generally hydrophobic molecules (or have parts that are hydrophobic)
- contain mostly carbon & hydrogen, few oxygen atoms, nitrogen, phosphorus

diverse group of molecules

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8
Q

What are the lipids roles?

A

1) Structure of cells
- Waterproof: keep insides in outsides out
- Pliable

2) Energy source
3) Communication (within cells & b/t cells)

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9
Q

What are the 5 types of lipids?

A

1) Fatty acids
2) Glycerides
3) Phospholipids & sphingolipids
4) Steroids
5) Eicosanoids

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10
Q

What are the protein chains of amino acids?

A
  • proteins are macromolecules
  • LINEAR chains of amino acids
  • there are 20 amino acids encoded by the universal genetic code
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11
Q

What is the protein R group & amino acid properties?

A
  • there are 20 AA’s encoded by the universal genetic code
  • of the 20, 9 are essential: need to consume them
  • 11 are non-essential: we can synthesize them
  • some AA’s are acidic, basic, polar, non-polar
  • “R groups”
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12
Q

What is the structure of proteins?

A
a short chain of AA is called a peptide
longer chains of AA are called proteins
- primary structure
- secondary structure
- tertiary structure
- quaternary structure

proteins have complex structures

  • determined by the sequence of AA’s that make them up
  • this sequence of AA’s is encoded in the genome
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13
Q

What are the 7 functional categories of proteins?

A
  1. Enzymes
  2. Membrane transporters
  3. Signal molecules
  4. Receptors
  5. Binding proteins
  6. Regulatory proteins
  7. Immunoglobulins
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14
Q

Protein binding definition

A

in order for a protein to DO SOMETHING, it must INTERACT WITH OR BIND TO other proteins, molecules or ions

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15
Q

What is the purpose of the ligand for protein binding?

A

protein binding is specific
- a molecule that binds to a protein binding site is called a LIGAND

  • an endogenous ligand is something natural in your body: for ex a hormone or neurotransmitter
  • non-endogenous may be a drug or toxin
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16
Q

What is affinity in terms of protein binding?

A

a protein binds a ligand with “affinity”

  • high affinity means it binds strongly
  • weak affinity means weak binding
17
Q

What is an agonist in terms of protein binding?

A

a ligand that binds to a protein binding site & alters the state of the protein, resulting in a biological response
- a hormone or neurotransmitter or a drug for ex

18
Q

What is an antagonist in terms of protein binding?

A

a ligand that reduces the action of an agonist (i.e. binds but causes NO biological response)
- also called inhibitors, blockers

19
Q

Competitive vs allosteric in terms of protein binding?

A

agonists & antagonists may be:

  • competitive: act to block the agonist normal binding site
  • allosteric: act to block a competitive agonist by binding to the protein away from the binding site & inactivate the binding site
20
Q

Protein binding has a ______ rate that depends on _____ and _______ ligand concentration & _______

A

measurable

protein
ligand

saturation

21
Q

Rate of protein binding can be modulated in which 5 ways?

A
  1. Isoforms (closely related proteins)
  2. Cofactors
  3. Activation/protein processing
  4. Physical factors
    - pH, temp
    * these can cause structural changes, proteins may become denatured
  5. Modulation
    - covalent modification
  6. phosphorylation & dephosphorylation
  7. addition of lipid or carbohydrate
  8. agonist/antagonist

or maybe just

  • binding regulatory subunits
  • phosphorylation by kinases
  • pH, temp