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IB Bio HL > B1.2 (Proteins) > Flashcards

B1.2 (Proteins) Flashcards

(61 cards)

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1
Q

Proteins

A

complex macromolecules composed of one or more chains of aminoacids

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2
Q

Amino acids

A

monomers that make up proetins

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3
Q

Components of a protein

A
  1. Amino Group
  2. Side chain (alpha carbon & R)
  3. Carboxyl Group
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4
Q

Formation of a peptide Bond

A

-COOH + -NH2 –> OC-NH + H20

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5
Q

Definition

Non Essential AA

A

can be produced by body

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5
Q

Definition

Essentials AA

A

cannot be produced by body

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6
Q

Examples

9 Essential AA

A

Histidine, Isoleucine, Lysine, leucine, Methionine, Phenylalamine, Threonine, Tryptophan and Vanine

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7
Q

Sources of protein

A

beans, lentils, meat, nuts, seeds

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7
Q

Uses of proteins

A
  • growth
  • repair
  • catalyst
  • structure (collagen)
  • transport (across membrane)
  • immunity
  • bidning sites for neurotransmitters
  • homeostasis (insulin)
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8
Q

Transcription

A

Dna -> mRna

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9
Q

Translation

A

mRna -> sequence of AA

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10
Q

Amount of Codons

A

64 Codons code for 20 AA

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10
Q

Codons

A

Three adjacent nucleotides in DNA or mRNA that code for a particular AA

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11
Q

Degenerate

A

Refers to the redundancy of genetic code (multiple codons code for the same protein)

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12
Q

Silent Mutations

A

Change in DNA sequence that does not result in the change of AA sequence of a protein

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13
Q

Nonesense mutation

A

A change in DNA sequence in which a stop codon is produced, ending the protein synthesis

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14
Q

Missense Mutation

A

Change in DNA arrengement as one nucleotide base is swapped causing a diferent AA sequnece

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15
Q

Frameshift Mutation

A

A change in DNA sequnece in which a nucletide is added or deleted resulting in triplet codons being read incorrectly

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16
Q

Polypeptides

A

A chain of AA which is linked together by peptide bonds

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17
Q

Lysozyme

A

enzyme that functions as a natural defense against bacterial infections by breaking down bacterial walls

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18
Q

Where is Lysozyme found

A

Salive and Tears

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19
Q

Alpha Neurotoxin

A

Binds to and inhibits receptors causing neuro toxic effects like paralysis and death

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20
Q

where is alpha neurotoxin found

A

snake venom

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21
Q

Glucagon

A

hormone which regulates blood sugar (low -> high)

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22
where is glucagon found
secreted from pancrease and released by the liver
23
Myoglobin
oxygen binding protein which facilitates the storage and release of O2 to muscle fibres
24
Denaturation
process in which the structure of a protein is irreversibly altered causing it to lose its function
25
How PH affects protein structure
The change in PH affects the charge on the protein molecule altering its activity so therefore its shape and solubility
26
What are the determinents of a proteins structure
the R group
26
How Temperature affects protein structure
The change in temperature breaks the hydrogen bonds holding the structure together meaning that the protein will unfold and lose its function
27
# Protein - Definition Primary structure
specific sequnece of AA that join to form polypeptide bonds
27
# Protein - Definition Quatenary Structure
arrangement & interaction of two or more polypeptide chains to form a functional protein
28
# Protein - Definition Secondary Structure
local folding patterns that occur within a polypeptide chain ## Footnote ex:
29
# Protein - Definition Tertiary Structure
gives rise to the overall three dimensional shape of the protein ## Footnote ex: integral proteins embedded in membranes: Rhodopsin in retinal cells which absorbs light
30
# Examples Examples of Fibrous Protein
* Keratin * Collagen
30
Globular Proteins
* spherical * irregular folds * water soluble * complex
31
Fibrous Proteins
* narrow * elongated * water insoluble * repeating structures
32
# Examples Examples of Globular Protein
* Pepsin * Haemoglobin * Insulin * Myoglobin
33
# Protein Structure Hydrogen bonds
* form between R Groups * hold distant regions of polypeptide chains together * maintains functional integrity
34
# Protein Structure Ionic bonds
* R group undergo binding/dissasociation of hydrogen ions * R groups interact with oppositely charged atoms in other molecules
34
Types of secondary protein folding patterns
Alpha helices and beta pleated sheets
34
# Protein Structure Disulfide Bridges
* between cysteine AA residues which contain sulfur atoms * form covalent bonds
35
# Protein Structure Hydrophobic interactions
* between non polar AA * as non polar dont interact with water = clump together * create hydrophobic clusters
36
Alpha helices
* H-Bond forms between amine group & -COOH * Every 4 Bond together * allows it to coil
37
important to remeber about hydrogen bonds
Hydrogen bonds are very weak intermolecular forces but they can be strong if they occur collectively
38
Beta pleated sheets
* H bonds form between adjacent strands (parallel) * pleated like structure * flat surface
39
conjugated proteins
globular proteins with a prospthetic group ## Footnote ex: Haemoglobin
40
prosthetic group
non polypeptide group that is required for biological functioning on the protein
41
non conjugated proteins
only polypeptide subunits ## Footnote ex: collagen (3) or Insulin (2)
42
Uses of globular proteins
enzymes, transport, regulators
43
fibrous proteins
support & stability to cells ## Footnote ex; bones, tissue, tendons
44
# Relating to protein stucture Insulin
* globular * binds to specific receptor cells to allow glucose to enter * hydrphilic exterior & phobic interior which allows interaction with water in blood * compact
45
Collagen
* fibrous * 2 polypeptide chains * hydroxyproline residues allows it to twist due to van-der-waals*
46
Van der Waals forces
weak intermolecular forces between atoms/molecules caused by temporary imbalance of electrons
47
quatenary protein examples
haemoglobin & rubisco (enzyme)
48
property of globular membrane protein
hydrophobic outside
49
property of globular water soluble protein
hydrophilic outside
50
Amount of AA combinations possible to form polypeptides
20 to the power of 20
51
Glycoproteins
Proteins with one or more carbohydrates attached to them
52
Amino acid polarity in membrane proteins
* polar= soluble, form stable interactions in water, strongly hydrophillic = form hydrophillic channels/pores * non polar = are soluble in lipid layer, hydrophobic
53
Cholesterol VS Steroids
Cholesterol = 4 ring + Hydrocarbon + OH => basis for making steroids Steroid = 4 ring + OH only

IB Bio HL (29 decks)

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