Protein (2) Flashcards

1
Q

=Biological catalyst
Ex. Pepsin, Trypsin

A

Enzymes

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2
Q
  • Include antibodies (immunoglobulins)which are specific protein molecules produced by specialized cells of the immune system in response to foreign antigens
A

Defense proteins

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3
Q
  • Another term for “antibodies”
    -essential in protecting against bacteria and viruses
A

Immunoglobulins

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4
Q

5 classes of antibodies

A
  1. IgM
  2. IgD
  3. IgA
  4. IgG
  5. IgE
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5
Q
  • Primary response to an antigen
  • first antibody produced by the fetus(mother to fetal).
  • biggest antibody
A

IgM

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6
Q

No biological effector function known

A

IgD

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7
Q

Antibody in secretions of saliva, tears, breast milk and mucosa

A

IgA

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8
Q
  • Smallest antibody
  • most abundant
  • has 4 isotopes ( IgG1, IgG2, IgG3, IgG4)
A

IgG

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9
Q
  • Associated with hypersensitivity reactions (allergies)
  • defense against parasite infections
  • found mainly in tissues
A

IgE

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10
Q

-Carry material from place to another in the body
Ex. Transferrin, Hemoglobin and Myoglobin

A

Transport protein

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11
Q
  • Controls many aspects of cell function,including metabolism and reproduction
    Ex. Insulin and Glucagon
A

Regulatory protein

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12
Q
  • Provide mechanical support to large animals and . provide them with their outer coverings
    Ex. Keratin
A

Structural protein

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13
Q
  • Are necessary for all forms of movement
    Ex. Actin and myosin, flagella of sperm cell
A

Movement proteins

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14
Q
  • Serves as source of amino acids for embryos or infant
    Ex. Albumin and casein
A

Nutrient protein

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15
Q

The amino acid sequence of protein is encoded in?

A

DNA

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16
Q

Proteins are synthesized by a series of steps called?

A

Transcription and Translation

17
Q

The use of a DNA strand to make a complimentary messenger RNA strand -mRNA

A

Transcription

18
Q

The mRNA sequence is used as a template to guide the synthesis of the chain of amino acids which make up the protein

A

Translation

19
Q

____can change by the process of mutation during the course of evolution

A

Genes

20
Q

____ can result in a change in the primary acid sequence of a protein

A

Mutation in gene

21
Q

2 types of secondary structure

A
  1. Alpha-helix
  2. Beta- Pleated Sheets
22
Q

The most common type of structure;may it be coiled of helical conformation

A

Alpha-Helix

23
Q

Every carbonyl oxygen is hydrogen bonded to amide hydrogen tour amino acids away in the chain

A
  • Special feature of alpha-helix
24
Q

Are structural proteins arranged in fibers or sheets that have only one type of secondary structure

A

Fibrous protein

25
Q

Are fibrous protein than form the covering (hairs,nails,fur) of most land animals

A

Alpha-Keratins

26
Q
  • Second common secondary structure in proteins resembles the pleated folds of drapery
  • involved in hydrogen bonds, and the polypeptide chain is nearly completely extended
A

Beta-Pleated Sheet

27
Q

2 Orientation of B-Pleated form

A
  1. Parallel
  2. Anti-Parallel
28
Q
  • Beta sheets which the polypeptide strands run in the same direction, N-terminus to C-terminus. (N-C)
  • Less stable because it forces the hydrogen bonds
    to occur at an angle, making them longer and thus weaker.
A

Parallel

29
Q
  • Beta sheets which the polypeptide strands run in opposite directions.
  • The N- terminus of one beta strand will be opposite the C-terminus of the other beta strand.
  • The hydrogen bonds are aligned directly opposite each other, making for stronger and more stable bonds.
A

Anti-parallel

30
Q
  • A protein whose structure is an antiparallel B-
    pleated sheet.
  • The polypeptide chains of a B-pleated sheet are almost completely extended, and silk does not stretch easily
A

Silk Fibroin

31
Q

Accounts for nearly half of the amino acids of silk fibroin

A

Glycine

32
Q

Account for most of the others content of silk fibroin

A

Alanine and Serine

33
Q
  • the complete three-dimensional (3-D) structure of a polypeptide.
  • formed spontaneously and stabilized both by side chain interactions, in extracellular proteins, by disulfide
    bonds.
    -This folding brings distant sequences in a linear polypeptide together into a stable structure
A

Tertiary Structure of Proteins

34
Q

-generally have a more compact and rounded shape and have functional roles (they do something)

A

Globular proteins

35
Q
  • some proteins are made up of multiple polypeptide
    chains, also known as subunits. When these subunits come together, they give the protein its ______
A

Quaternary Structure

36
Q

– when a non-protein group is added to the functional protein.
Ex: Glycoprotein

A

Prosthetic Group

37
Q
  • Is the degradation of protein by cellular enzymes
    in a process called hydrolysis.
    -The macromolecules are the proteins or
    polypeptides themselves, and the subunits are the
    amino acids.
A

Protein Digestion

38
Q

Protein Digestion takes place in 2 different phases:

A
  • In the stomach
  • In the small intestine
39
Q

Both of these phases of digestion are based on
several types of enzymes that are called

A

Proteinases and Proteases