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biochem > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

a naturally-occurring, unbranched polymer in which the monomer units are amino acids

A

protein

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2
Q

average nitrogen content of proteins _____ BY MASS

A

15.4%

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3
Q

contains one peptide chain

A

Monomeric

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4
Q

contains more than one peptide chain

A

Multimeric

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5
Q

A protein in which only amino acid residues are present

-Composed of amino acids without prosthetic groups

A

Simple proteins

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6
Q

A protein that has one or more non-amino acid entitles (prosthetic groups) present in its structure

A

Conjugated protein

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7
Q

bonds that connect on amino acid to another is known as

A

amide / peptide bonds

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8
Q

structure of protein refers to the order in which amino acids are linked together in a protein

A

Primary structure

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9
Q

He sequenced and determined the primary
structure for the first protein - Insulin

A

Frederick Sanger

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10
Q
  • Arrangement of atoms of backbone in space.
  • The two most common types : alpha-helix (a-helix) and the beta-pleated
    sheet (b-pleated sheet).
  • Determines interaction of adjacent amino acids
A

SECONDARY STRUCTURE

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11
Q

A single protein chain adopts a
shape that resembles a coiled spring

A

Alpha-helix (a-helix)

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12
Q
  • Completely extended
    amino acid chains
A

Beta-pleated sheets

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13
Q
  • The overall three-dimensional shape of a protein
  • Results from the interactions between amino acid side chains (R groups) that are widely separated from each other.
A

TERTIARY STRUCTURE

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14
Q

covalent, strong, between two cysteine groups

A

Disulfide bond

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15
Q

Salt Bridge between charged side chains of acidic and
basic amino acids

A

Electrostatic interactions

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16
Q

acidic and/or basic R groups

A

H-Bonding between polar

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17
Q

Between non-polar side chains

A

Hydrophobic interactions

18
Q
  • HIGHEST level of protein organization
    -The subunits are held together mainly by hydrophobic interactions
    between amino acid R groups.
A

QUATERNARY STRUCTURE

19
Q
  • Most abundant proteins in humans (30% of total body protein)
  • Major structural material in tendons, ligaments, blood vessels,
    and skin
  • Organic component of bones and teeth
  • Predominant structure - triple helix
  • Rich in proline (up to 20%) – important to maintain structure
A

Fibrous Proteins: Collagen

20
Q
  • An oxygen storage molecule in muscles.
  • Monomer - single peptide chain with one heme unit
  • Binds one O2 molecule
  • Has a higher affinity for oxygen than hemoglobin.
  • Oxygen stored in myoglobin molecules serves as a reserve
    oxygen source for working muscles
A

Globular Proteins: Myoglobin

21
Q
  • An oxygen carrier molecule in blood
  • Transports oxygen from lungs to tissues
  • Tetramer (four peptide chains) - each subunit has a heme group
  • Can transport up to 4 oxygen molecules at time
  • Iron atom in heme interacts with oxygen
A

Globular Proteins: Hemoglobin

21
Q

PROTEINS CLASSIFICATION BASED ON FUNCTION

A

-bind small molecules
- bind other proteins and form fiber-like structures
-integrated into cell membranes

22
Q
  • Enzymes are best known for their catalytic role.
  • Almost every chemical reaction in the body is driven by an enzyme
A

Catalytic proteins

23
Q

Immunoglobulins or antibodies are central to functioning of the body’s immune system.

A

Defense proteins

24
Q

Bind small biomolecules, e.g., oxygen and other ligands, and transport them to other locations in the body and release them on
demand.

A

Transport proteins

25
Q

transmit signals to coordinate biochemical processes between different cells, tissues, and organs.

A

Messenger proteins

25
Q
  • Necessary for all forms of movement.
  • Muscles contain filament-like contractile proteins (actin and myosin).
  • Human reproduction depends on the movement of sperm
A

Contractile proteins

26
Q

Confer stiffness and rigidity

A

Structural proteins

27
Q

Bind (and store) small molecules.

A

Storage proteins

27
Q

Span a cell membrane and help control the
movement of small molecules and ions.

A

Transmembrane proteins

28
Q

Often found “embedded” in the exterior surface of cell membranes - act as sites for receptor molecules

A

Regulatory proteins

29
Q

Particularly important in the early stages of life - from embryo to infant.

A

Nutrient proteins

30
Q
  • Results in the generation of an amine and a carboxylic acid functional groups.
  • Free amino acids produced are absorbed into the bloodstream and transported to the liver for the synthesis of new proteins.
A

PROTEIN HYDROLYSIS

31
Q
  • Partial or complete disorganization of protein’s tertiary structure
  • Cooking food denatures the protein but does not change protein nutritional
    value
A

PROTEIN DENATURATION

32
Q

produced as a protective response to the invasion of microorganisms or foreign molecules - antibodies against antigens.

A

Glycoproteins

33
Q

bonding to an antigen via variable region of an immunoglobulin occurs through hydrophobic interactions, dipole
– dipole interactions, and hydrogen bonds.

A

Immunoglobulin

34
Q
  • a conjugated protein that contains lipids in addition to amino acids
  • help suspend lipids and transport them through the bloodstream
A

LIPOPROTEINS

35
Q

Transport dietary triacylglycerols from intestine to liver
and to adipose tissue.

A

Chylomicrons

36
Q

Transport triacylglycerols
synthesized in the liver to adipose tissue.

A

Very-low-density lipoproteins (VLDL)

37
Q

Transport cholesterol synthesized in the
liver to cells throughout the body.

A

Low-density lipoproteins (LDL)

38
Q

Collect excess cholesterol from body
tissues and transport it back to the liver for degradation to bile acids.

A

High-density lipoproteins (HDL):

biochem (7 decks)

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