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

B1.2 (Proteins) Flashcards

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Biology 101 flashcards
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

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, maintenance

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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 partocular AA

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11
Q

Degenerate

A

Refers to the redundancy of genetiuc 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 whichbis 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

20
Q

where is alpha neurotoxin found

A

snake venom

21
Q

Glucagon

A

hormone hwihc regulted blood sugar (low -> high)

22
Q

where is glucagon found

A

secreted from pancrease and released by the liver

23
Q

Myoglobin

A

oxygen binding protein which facilitates the storage and release of O2 to muscle fibres

24
Q

Denaturation

A

process in which the structure of a protein is irreversibly altered causing it to lose its function

25
Q

How PH affects protein structure

A

The change in PH affects the charge on the protein molecule altering its activity so therefore its shape and solubility

26
Q

What are the determinents of a proteins structure

A

the R group

26
Q

How Temperature affects protein structure

A

The change in temperature breaks the hydrogen bonds holding the structure together meaning that the protein will unfold and lose its function

27
Q

Protein - Definition

Primary structure

A

specific sequnece of AA that join to form polypeptide bonds

27
Q

Protein - Definition

Quatenary Structure

A

arrengemnt & interaction of two or more polypeptide chains to form a functional protein

28
Q

Protein - Definition

Secondary Structure

A

local folding patterns that occur within a polypeptide chain

ex:

29
Q

Protein - Definition

Tertiary Structure

A

gives rise to the overall three dimensional shape of the protein

ex: integral proteins embedded in membranes: Rhodopsin in retinal cells which absorbs light

30
Q

Examples

Examples of Fibrous Protein

A
  • Keratin
  • Collagen
30
Q

Globular Proteins

A
  • spherical
  • irregular folds
  • water soluble
  • complex
31
Q

Fibrous Proteins

A
  • narrow
  • elongated
  • water insoluble
  • repeating structures
32
Q

Examples

Examples of Globular Protein

A
  • Pepsin
  • Haemoglobin
  • Insulin
  • Myoglobin
33
Q

Protein Structure

Hydrogen bonds

A
  • form between R Groups
  • hold distant regions of polypeptide chains together
  • maintains functional integrity
34
Q

Protein Structure

Ionic bonds

A
  • R group undergo binding/dissasociation of hydrogen ions
  • R groups interact with oppositely charged atoms in other molecules
34
Q

Types of secondary protein folding patterns

A

Alpha helices and beta pleated sheets

34
Q

Protein Structure

Disulfide Bridges

A
  • between cysteine AA residues which contain sulfur atoms
  • form covalent bonds
35
Q

Protein Structure

Hydrophobic interactions

A
  • between non polar AA
  • as non polar dont interact with water = clump together
  • create hydrophobic clusters
36
Q

Alpha helices

A
  • H-Bond forms between amine group & -COOH
  • Every 4 Bond together
  • allows it to coil
37
Q

important to remeber about hydrogen bonds

A

Hydrogen bonds are very weak intermolecular forces but they can be strong if they occur collectively

38
Q

Beta pleated sheets

A
  • H bonds form between adjacent strands (parallel)
  • pleated like structure
  • flat surface
39
Q

conjugated proteins

A

globular proteins with a prospthetic group

ex: Haemoglobin

40
Q

prosthetic group

A

non polypeptide group that is required for biological functioning on the protein

41
Q

non conjugated proteins

A

only polypeptide subunits

ex: collagen (3) or Insulin (2)

42
Q

Uses of globular proteins

A

enzymes, transport, regulators

43
Q

fibrous proteins

A

support & stability to cells

ex; bones, tissue, tendons

44
Q

Relating to protein stucture

Insulin

A
  • globular
  • binds to specific receptor cells to allow glucose to enter
  • hydrphilic exterior & phobic interior which allows interaction with water in blood
  • compact
45
Q

Collagen

A
  • fibrous
  • 2 polypeptide chains
  • hydroxyproline residues allows it to twist due to van-der-waals*
46
Q

Van der Waals forces

A

weak intermolecular forces between atoms/molecules caused by temporary imbalance of electrons

IB Bio HL (5 decks)

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