Amino Acids, Peptides, and Proteins Flashcards

1
Q

Fibrous Proteins

A
  • have polypeptide chains organized in long fibers/sheets
  • physically tough, but can still be slightly stretchy
  • water insoluble
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2
Q

Structural proteins

A
  • Fibrous protein that functions in support
  • Collagen and elastin are used in tendons and ligaments of animals
  • Silk fibers for insect webs
  • Keratin is found in hair horns and feathers
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3
Q

Contractile

A
  • Fibrous protein that specializes in movement
  • Actin and myosin contract in order to form a cleavage furrow and allow muscles to move
  • Move cilia and flagella
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4
Q

Globular Proteins

A
  • Chains folded into compact, rounded shapes
  • Extremely soluble in aqueous solutions
  • Can act as storage protein fo AAs
  • Can act as transport protein (ex: hemoglobin)
  • Can act as enzymes
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5
Q

Amino Acids

A

Amino acid sequence, composition, and amount help distinguish proteins from one another (i.e determine primary protein structure and in turn protein function)

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6
Q

General amino acid structure

A

central (alpha) carbon, amino group, carboxylate group, H atom, R group

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7
Q

Immune system proteins

A
  • globular proteins

- antibodies help fight bacteria and viruses

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8
Q

Peptides

A

Amino acid polymers of 50 or less

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9
Q

Polypeptides/protein

A

Amino acid polymers greater than 50

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10
Q

Phenylalanine (Phe)

A
  • Essential
  • Nonpolar
  • R group is benzene derivative
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11
Q

Valine (Val)

A
  • Essential
  • Nonpolar
  • R group is CH connected to two methyl groups
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12
Q

Threonine (Thr)

A
  • Essential
  • Polar
  • R group is C connected to H, CH3 and OH
  • Contain hydroxyl
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13
Q

Methionine (Met)

A
  • Essential
  • Nonpolar
  • R group is 2 CH2’s then S then CH3
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14
Q

Leucine (Leu)

A
  • Essential
  • Nonpolar
  • R group is CH2 connected to CH connected to 2 CH3’s
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15
Q

Isoleucine (Ile)

A
  • Essential
  • Nonpolar
  • R group is C connected to H and CH3 and CH2 connected to CH3
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16
Q

Lysine (Lys)

A
  • Essential
  • Basic
  • Polar
  • R group is 4 carbon chain with NH+
17
Q

Histidine

A
  • Essential
  • Basic
  • Polar
  • R group is CH2 connected to pentagonal shape with N and C
  • Weak base because only alpha NH3+ is protonated
18
Q

Arginine

A
  • Conditional
  • Basic
  • Polar
  • R groups is 3 carbon chain with last C connected to N connected to H and C connected to NH2 and double bonded to NH2+
19
Q

Zwitterions

A
  • Neutral form of amino acid
  • Exist at different pH’s for different amino acids depending on pKa
  • R group primarily gives amino acid its unique properties
20
Q

Amino acid classes

A

Classified by R groups ability to interact with water

21
Q

Titration of amino acids

A

-Free amino acids contain ionizable groups, form depending on pH

22
Q

pI

A

Isoelectric point; average of two pKas either side of zwitterion

23
Q

Good buffers

A
  • Weak acids or bases
  • Best in solutions within 1 pH unit on either side of one of their pKa values
  • Higher buffer concentration= greater buffering capacity
24
Q

Bonds broken when protein denatures

A
  • Hydrogen bonds
  • Hydrophobic interactions
  • Salt bridges
25
Q

Lipid functions

A
  • Key source for endurance activities
  • Insulation and water resistance
  • Components of biomembranes
  • Derivatives of other biomolecules
26
Q

Saturated fatty acids

A
  • Highly flexible molecules; free C-C rotation
  • Fully extended conformation is most stable due to least amount of steric hindrance
  • As molecular mass increases, so does melting point