Module 1B - Biomolecules and Enzymes Flashcards

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1
Q

structurally complex and
functionally sophisticated
molecules

A

THE SHAPE AND STRUCTURE
OF PROTEINS

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2
Q

The Shape of a Protein Is Specified by Its ____ ___Sequence

A

Amino Acid

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3
Q

How many amino acids are there

A

20 amino acids

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4
Q
  • made of long
    unbranched chain of
    these amino acids
  • polype
A

Shape of protein

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5
Q

-repeating sequence of
atoms along the core of
the polypeptide chains

A

polypeptide backbone

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6
Q

give amino
acids its unique properties

A

Side chains

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7
Q

Polar amino acids

A

arginine
asparagine
aspartic acid (or aspartate), glutamine
glutamic acid (or glutamate), histidine
lysine
serine
threonine
Tyrosine

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8
Q

Non-polar amino acid (all non-polar side chain)

A

alanine
cysteine
glycine
isoleucine
leucine
methionine
phenylalanine
proline
tryptophan
valine

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9
Q

2 polar amino acid that has negative side chain

A

Aspartic acid and Glutamic acid

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10
Q

3 polar amino acid that has positive side chain

A

Arginine
Lysine
Histidine

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11
Q

5 polar amino acid that has uncharged polar

A

Asparagine
Glutamine
Serine
Threonine
Tyrosine

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12
Q

week
noncovalent
bonds

A

Protein folding

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13
Q

3 weak noncovalent bonds

A

hydrogen
bonds
electrostatic
attractions
van der Waals

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14
Q

tend
to be forced together in an
aqueous environment to
minimize their disruptive
effect on the hydrogen-bonded network of water
molecules

A

hydrophobic molecules,
including the nonpolar side
chains of amino acids

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15
Q

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

A

Amino acids

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16
Q

Assist in the protein folding

A

Molecular chaperones

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17
Q

2 Common Folding Patterns

A

The a Helix and the β Sheet

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18
Q

Folding pattern in protein result from hydrogen-bonding between ___-__ and __=__
in the polypeptide
group

A

N-H and C=O groups

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19
Q

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

A

Parallel chains

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20
Q

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

A

antiparallel chains

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21
Q

generated when a single
polypeptide chain twists around
on itself to form a rigid cylinder

A

a helix

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22
Q

hydrogen bonds between every
___ peptide – linking C=O of one
peptide bond to N-H of another

A

4th

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23
Q

formed from two or
more have most of their nonpolar
side chains on one side

A

coiled-coil

24
Q

Modular Units from
Which Larger Proteins Are Built

A

Protein domains

25
Q

Primary structure of protein

A

Amino acid sequence

26
Q

Secondary structure of protein

A

hydrogen bonding of the peptide
backbone; helices and β sheets

27
Q

tertiary structure of protein

A

full 3D organization of a polypeptide chain

28
Q

Quaternary structure of protein

A

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

29
Q

has been
more highly conserved
than the amino acid
sequence

A

the structure of the
different members of a
protein family

30
Q
  • regulatory proteins in the
    homeodomain family4
  • identical in only 17 of 60 aa
    residues
A

yeast 2 protein and the
Drosophila engrailed
protein

31
Q

protein families are readily recognized when the ___ of any organism is
sequenced

A

genome

32
Q

human genome = ____ protein-coding genes

A

21,000

33
Q

40% of our protein-coding genes to
known protein structures, ___ diff
families

A

500

34
Q

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

A

Protein domains

35
Q

process of
creating new combination of
gene functional domains

A

Domain shuffling

36
Q

– subset of
protein domains, mobile
during evolution

A

protein modules

37
Q

easily
integrated into other proteins

A

Protein domains

38
Q

can be readily linked in
series to form extended
structures

A

Domains

39
Q

What is domain specialized functions

A

Major Histocompatibility Complex (MHC) antigen-recognition domain – only in humans

40
Q

have inherited
nearly all of their protein
domains from invertebrates –
7% identified human domains
being vertebrate-specifics

A

Vertebrate

41
Q

has given
rise to many novel
combinations of protein
domains

A

domain shuffling during
vertebrate evolution

42
Q

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

A

weal noncovalent bonds

43
Q

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

A

binding site

44
Q

forming
a symmetric complex of two protein
subunits (dimer)

A

“head-to-head” arrangement

45
Q

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

A

hemoglobin

46
Q

a long chain of identical
protein molecules can be
constructed if each molecular
has a ___ __
complementary to another
region of the surface of the
same molecule

A

binding site

47
Q

long helical
structure produced from many
molecules of the protein actin

A

actin filament

48
Q

why is a helix a common
structure in biology?

A

all subunits are identical, they
can only fit together in one
way – rarely straight line –
resulting in a helix (resembles
a staircase

49
Q

Protein Molecules Have Elongated,
Fibrous Shapes

A

-fibrous protein
- keratin filaments
- a-keratin
- intermediate filaments

50
Q

elongated three-dimensional
structure

A

Fibrous protein

51
Q

main component in long
lived structures

A

Keratin filaments

52
Q

a dimer of two identical subunits

A

keratin

53
Q

rope-like structures; important component of the cytoskeleto

A

intermediate filaments

54
Q
  • abundant outside
    the cell
  • main
    component of the
    gel-like extracellular
    matrix
A

Fibrous protein

55
Q

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

A

collagen

56
Q

collagen consists
of three long
polypeptide chains,
each containing
that nonpolar
amino acid ____
at every ___ position

A

glycine
3rd

57
Q
A