IB: Proteins Flashcards

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1
Q

made of long unbranched chain of these amino acids

A

Protein

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2
Q

a linear chain of amino acids

A

polypeptides

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3
Q

repeating sequence of atoms along the core of the polypeptide chains

A

Polypeptide backbone

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4
Q

give amino acids its unique properties

A

side chains

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5
Q

involved in protein folding

A

weak covalent bonds

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6
Q

Types if if weak noncovalent bonds on protein folding

A

-Hydrogen bonds
-electrostatic attrations
- Van der Waals

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7
Q

contains all the information needed for specifying the three-dimensional shape of a protein

A

amino acid sequence

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8
Q

assist in protein folding

A

Molecular chaperones

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9
Q

Common folding patterns

A
  • α helix
  • β-sheet
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10
Q

Types of folding that leads to α-helix and β-sheet folding patterns?

A

Hydrogen bonding between N-H and C=O groups

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11
Q

Types of β-sheet structures

A
  • Parallel chains
  • antiparallel chains
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12
Q

form from neighboring segments of the polypeptide backbone that run in the same orientation

A

parallel chains

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13
Q

-from a
polypeptide backbone that folds
back and forth upon itself
-each section of the chain running in the direction opposite of that of its immediate neighbors

A

Antiparallel chains

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14
Q

Formation of α-helix

A
  • when single polypeptide chain twist around on it self to form rigid cylinder
    -Hydrogen bonds between every 4th peptide
    -coiled-coil form
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15
Q

4 levels of protein structure

A
  • Primary structure
  • secondary structure
  • tertiary structure
  • Quaternary structure
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16
Q

amino acid sequence

A

primary structure

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17
Q

hydrogen
bonding of the peptide
backbone; α helices and β sheets

A

Secondary structure

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18
Q

full 3D
organization of a polypeptide chain

A

tertiary structure

19
Q

protein
molecule formed as a complex of more than one polypeptide chain

A

Quaternary structure

20
Q

How are protein classified?

A

Based on their tertiary structure

21
Q

used to see structure of protein

A

X-ray crystallography

22
Q

the basic units of proteins that can fold,
function, and evolve independently

A

Protein domains

23
Q

process of
creating new combination of gene functional domains

A

domain shuffling

24
Q

subset of protein domains, mobile during evolution

A

protein modules

25
Q

only in humans, the reason why humans cant receive blood from other organisms

A

MHC (Major Histocompatibility Complex)

26
Q

allow proteins to bind to each other to produce
structures in the cell

A

Weak noncovalent bonds

27
Q

any region of a protein’s surface that can interact with another molecule

A

binding site

28
Q

forming a symmetric complex of two protein subunits (dimer)

A

“Head-to-head” arrangement

29
Q

two identical α-globin
subunits and two identical β-globin subunits, symmetrically arranged

A

Hemoglobin

30
Q

long helical structure produced from many molecules of the protein actin

A

actin filament

31
Q

a long chain comprised of identical protein molecule

A

Filaments

32
Q

Why is alpha helix common?

A

All subunits are identical
- can only fit together in one way

33
Q

Types of protein molecule shapes

A

-Fibrous protein
-Elongated protein

34
Q

elongated three-dimensional structure

A

fibrous protein

35
Q

example of fibrous protein

A
  • keratin filaments
  • a(alpha) keratin
36
Q

ropelike structures;
important component of the cytoskeleton

A

intermediate filaments

37
Q

consists of three long polypeptide chains
- each containing that nonpolar amino acid glycine at every 3rd position

A

collagen

38
Q

Another abundant protein in ECM
- highly disordered polypeptide

A

Elastin

39
Q

causes of disordered polypeptide chain

A
  • To form specific binding sites for other protein
  • Trigger cell signaling
  • Restrict diffusion
  • Serves as tether to hold two domains
40
Q

act as atomic staple
stabilize monomeric and multisubunit proteins

A

S-S bonds (Disulfide bonds)

41
Q

Advantages of subunits

A

-requires only small amount of genetic information
- assembly and disassembly
- error in synthesis can be avoided easily

42
Q

example of subunit

A

capsid of viruses

43
Q

made of identical protein subunits that enclose and protect viral nucleic acid

A

Capsid of viruses

44
Q

Guide construction but take no part in the final assembled structure

A

Assembly factors