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Biology with Lynette > Amino Acids + Proteins > Flashcards

Amino Acids + Proteins Flashcards

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1
Q

What are Proteins?

A
  • Linear polymers of amino acids.
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2
Q

Amino Acids (Read)

A
  • 20 diff common AA
  • 10 essential
  • 10 non - essential
  • Conc of free AA in cell is low.
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3
Q

Can amino acids be stored in the body?

A
  • No
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4
Q

What are Amino Acids needed for?

A
  • To meet the body’s requirement for protein.
  • Synthesize new proteins
    synthesis as precursors for other compounds.
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5
Q

What can the bacteria E.coli do?

A
  • Synthesize a set of standard AA.
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6
Q
  • How does the body convert proteins to AA’s in the digestive system?
A
  • By releasing proteolytic enzymes.
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7
Q

What does the basic structure of an Amino Acid contain?

C.A.H.R

A
  • Carboxyl Group
  • Amino Group
  • Hydrogen atom
  • Side Chain ( R group)

All are attached to a central carbon atom known as the α-carbon.

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8
Q

How does the R Group (side chain) vary?

A
  • Size
  • Shape
  • Charge
  • Solubility

The properties of the side chain(s) influence the overall 3D shape (configuration of a protein). The 3 D shape plays an integral part in protein functionality.

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9
Q

What can the R Group (side chain) be?

A 
▪ Aliphatic (non-polar)
▪ Aromatic (ring structure, generally non-polar)
▪ Polar
▪ Negatively charged
▪ Positively charged
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10
Q

What is an Aromatic Compound?

A
  • An organic compound made of C + H, contains an aromatic ring configuration of atoms.
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11
Q

Give an example of an Aromatic compound.

A
  • Benzene
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12
Q

What is an Aliphatic Compound?

A
  • An organic compound made of C + H, it is Non- Aromatic.
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13
Q

Give examples of Aromatic Amino Acids. (P.T.T)

A
  • Tyrosine
  • Tryptophan
  • Phenylalanine
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14
Q

How do you test for the detection of proteins?

A
  • Spectrophotometry @ λ max 280
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15
Q

What is a Peptide?

A
  • Short chain of AA monomer.
  • Linked by peptide bonds
  • 2 - 20 AA’s

Shortest peptide is a dipeptide, then tripeptide, tetrapeptide etc.

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16
Q

What are Peptide bonds also called?

A
  • Amide Bonds
17
Q

What is a Polypeptide?

A
  • Long, continuous, unbranched peptide chain

- 20 - 50 AA’S

18
Q

What is a protein?

A
  • One or more polypeptides arranged in a biologically functional way.
  • 50 - ? AA’s
19
Q

How are Amino Acids added added to a linear polymer in a stepwise manner?

A
  • By a Condensation Rxn ( loss of H2O).
20
Q

Read

A

▪ As H2O is removed, the carboxyl
carbon of one AA and the amino nitrogen of a second are linked directly.

▪ This covalent C—N bond linking two AA’s is known as a peptide bond, shown below in bold.

▪ Formation consumes energy – living systems – ATP.

▪ Bond can be broken by hydrolysis (the adding of water) which releases
energy.

21
Q

Give 5 examples of the biological functions of Peptides. ( V.O.L.A.B)

A
  • Vasopressin (H20 Reabsorption)
  • Oxytocin ( Uterine Contraction)
  • LHRH (Fertility)
  • Angiotensin II (Reg. Blood Pressure)
  • Bradykinin ( Inhibits Inflammation)
22
Q

How are Amino Acids linked?

A
  • Covalently linked by peptide bond

- Linear sequence

23
Q

How many levels of structure do proteins have?

Name these levels.

A
  • 4
  • Primary
  • Secondary
  • Tertiary
  • Quaternary
24
Q

What is the primary structure of a protein?

A
  • The linear sequence of amino acids within a protein.

- Dictated by the Genetic Code.

25
Q

What is the Secondary Structure of a protein?

A
  • Occurs due to Hydrogen Bonding between peptide bonds along the length of the protein.
  • Causing a Localized Helix to form + sheet structure.
26
Q

What do hydrogen bonds do to the secondary protein structure?

A
  • They stabilize the structure.
27
Q

What is the Tertiary structure of a protein?

A
  • Caused from extensive folding a polypeptide chain into a closely packed (almost) spherical shape.
28
Q

What is the extensive folding in the tertiary structure caused by?

A
  • Chemical interactions between the side chains of the amino acids.
29
Q

What is the most protein structure/Conformation and why?

A
  • Tertiary Structure

- Bc of the chemical interactions between the side chains of the amino acids stabilize the structure.

30
Q

Read

A

▪ H bonding between side chains
▪ Ionic bonding between side chains with ionizable groups.
▪ Disulphide bonds between 2 cysteine residues (Cys - S - S - Cys)
▪ Hydrophobic interactions ; this is
the most significant tertiary structure stabilization force. It constitutes a non covalent interaction between the non
polar R Groups.

31
Q

Quaternary structure?

A

▪ Limited to proteins with multiple
polypeptide sub units . Each sub unit is a separate polypeptide chain.

▪ The bonds and forces that maintain
quaternary structure are the same
as those responsible for tertiary
structure.

32
Q

Give an example of a protein with a Quaternary structure?

A
  • Hemoglobin, the oxygen carrying

protein in blood.

33
Q

Biological Functions of Proteins.

A
  • Enzymes - many proteins function as enzymes i.e. biochemical catalysts.
  • Hormones; many regulate biological/biochemical functions in target tissue e.g. hormones.
  • Some bind other molecules for storage and transport e.g. hemoglobin binds 0 2 , CO 2 in erythrocyte cells (red blood cells).
  • Structural proteins provide support and shape to cells & therefore to tissue and organisms (skin, tendons, hair (Elastin, Collagen , Keratin).
  • Assemblies of proteins perform mechanical work ( flagella, cilia , Some proteins are hormones they regulate biochemical activities in target cells or tissue.
  • Proteins also serve a range of other specialized functions including their defense functions as immunoglobulin (antibodies).
34
Q

Industrial Uses of Proteins.

A
  • Enzymes: (proteases) meat tenderization, cheese manufacture rennin, contact lens cleaner.
  • Regulatory Protein medical uses, insulin diabetes, growth hormone treat dwarfism, FSH treat infertility.
  • Antibodies covid 19 test, HIV test, pregnancy test, Ovulation test.

Biology with Lynette (11 decks)

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