Biology Exam 1 Lecture 3 Flashcards

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1
Q

_____ is an excellent “example” protein

A

Hemoglobin

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2
Q

hemoglobin is a ____ in which each subunit binds a ___ group which then binds an _____

A

heterotetramer, heme, oxygen

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3
Q

Proteins fold into conformations that represent ___

A

energy minima

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4
Q

Unfolded proteins are said to be ____

A

denatured

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5
Q

____ in the cell help proteins fold into their correct conformations

A

Molecular chaperones

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6
Q

What are the 4 levels of structural organization in proteins?

A

Primary- linear amino acid sequence
Secondary- folding patterns
Tertiary- 3D organization of secondary structures, Protein domains
Quaternary- organization of protein complexes

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7
Q

A protein’s structure will be determined by its ____.

A

primary sequence.

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8
Q

Relevant parts of the protein will be the ____ and the side chains or ___ of each specific amino acid.

A

polypeptide backbone, R-groups

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9
Q

Which of the four types of amino acids is represented by the most members?

A

Non-polar

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10
Q

Proteins can fold into many possible ____,
however energetics drives them to ___ ____ _____
for each protein. Folding starts _____

A

conformations, one stable one, co-translationally

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11
Q

_____ bonds serve to generate structure
in proteins. These can occur between R groups or parts of the polypeptide backbone

A

Weaker, non-covalent

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12
Q

In cells different _____
help to fold and refold proteins

A

chaperones

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13
Q

_____ interactions will often help to drive interactions placing non-polar groups
near the ____ of the protein’s structure.

A

water, center

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14
Q

Modifications like N- and
O-linked ____ can
influence structure

A

glycosylation

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15
Q

In the cytosol, which sequence of amino acid side chains would most likely be found in the interior structure of a globular protein?

uncharged polar – hydrophobic – basic
basic – basic – hydrophobic
nonpolar – nonpolar – nonpolar
acidic – acidic – uncharged polar
They are all equally likely to be on the protein’s outside

A

nonpolar – nonpolar – nonpolar

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16
Q

____in proteins are part of _____
They are often arrangements of linked regions of alpha helices and beta sheets.

A

Domains, tertiary structure

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17
Q

______ between domains can
provide a variety of functions

A

Unstructured regions

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18
Q

what is the favored conformation when all of the R groups locally
are hydrophobic?

A

alpha helices

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19
Q

A protein’s primary structure is dependent upon _____ bonds that _____.

A

peptide; link adjacent amino acids

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20
Q

Z-Mapp is a drug treatment used for Ebola – what is it?

A

A “cocktail” of inhibitory antibodies

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21
Q

____ can form _____ ____ ______, which can
help stabilize protein structures in harsh environments.

A

Cysteines, covalent disulfide bridges

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22
Q

Antibodies contain many intra- and inter-polypeptide _____ that help maintain their conformations

A

disulfide bridges

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23
Q

Two other extracellular proteins containing many disulfide
bridges

A

collagen and elastin

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24
Q

Non-protein components of proteins -

A

retinal (rhodopsin), heme (hemoglobin)

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25
Q

A common theme in cells is ___ ____of subunits
into a ____ - this is particularly true with regard to
cytoskeletal proteins

A

dynamic assembly, filament

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26
Q

Weaker, non-covalent bonds also are key to specific _____ binding of proteins. This occurs through the formation
of _____.

A

ligand, binding sites

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27
Q

Specific membrane compartments such as lysosomes and peroxisomes can be isolated from cell lysates by differential centrifugation? T or F

A

True

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28
Q

Gel filtration chromatography:

A

Can separate proteins based on size/shape

29
Q

Different _____ ______ ______
have different separation properties that will cause proteins to interact with them in distinct ways. This allows using different columns to either bind and concentrate a protein or exclude it while binding other contaminating proteins.

A

column chromatography matrices

30
Q

True/False: Two ways that antibodies can be used for immunodetection of cellular proteins are:

  1. By decorating them with gold particles to enable their visualization in EM when bound to cell proteins
  2. By labeling them for use in detecting proteins extracted from cells and separated on gels then blotted to membranes (so called immunoblot)
A

True

31
Q

The structure or conformation of a protein can be predicted by certain methods and also empirically determined by biochemical methods such as ____ and _____ as well as enzymatic methods.

A

NMR, X-Ray crystallography

32
Q

Antibodies are highly useful for…

A

detection and purification of specific proteins

33
Q

______ is now a very commonly used method of determining protein identity
and modification ______

A

Mass spectrometry, proteomics

34
Q

Proteins can be studied by mass spectrometry – in this method:

A

Proteins are fragmented and sized to identify them

35
Q

Ribozymes are…

A

Catalytic RNA molecules thatact as enzymes

36
Q

Prions:

A

Proteinaceous Infectious Particles

37
Q

Prion Diseases:

A

Spongiform Encephalopathies, Bovine spongiform encephalopathy

38
Q

Prion Properties:

A

Transmissible
No nucleic acid component
Species barriers
Protein present in normal cells

39
Q

Protein conformation changes underlie prion formationand formation of ____

A

amyloid fibers

40
Q

Prions, commonly denoted PrPSc,
can ____ their conformation to
cellular PrP

A

template

41
Q

Spongiform encephalie

A

Formation of protein aggregates
or plaques in brain cells,
these lead to lysosomal lysis
and the formation of holes
in tissues where now dead cells
once resided.

42
Q

_____and _____ carry out the reversible modification of many substrate proteins

A

Protein kinases, phosphatases

43
Q

T/F : Phosphorylation of some substrates by protein kinases can serve to inactivate protein functions.

A

True

44
Q

For proteins regulated by GTP/GDP binding, it is the case that:

A

GTP is bound to the protein and converted to GDP + Pi as it acts on another protein.

The protein with GDP bound releases GDP and then binds a new molecule of GTP to do another cycle of regulation

45
Q

The ____ level or _____ of any individual species of protein in the cell will be a unique function of the factors controlling both its ____ (production) and _____ (destruction).

A

steady state, concentration

synthesis, degradation

46
Q

The half-life of a protein is half the average number of minutes (or hours) the protein spends in the cell. This can be determined by a ____

A

pulse-chase experiment.

47
Q

Proteins originate on ____ or on ____

A

free ribosomes, ribosomes directed to the ER

48
Q

Misfolded proteins in the cell can be degraded by what structures?

A

Proteasomes

49
Q

The posttranslational modification that targets proteins to the proteasome is?

A

Ubquitylation

50
Q

what are Proteasomes?

A

Proteasomes are multi-protein complexes found in the cytosol and nucleus

51
Q

what do proteasomes do?

A

They function to receive and degrade cellular proteins that are damaged or that have been specifically targeted for degradation by modification with ubiquitin.

52
Q

What are Lysosomes?

A

Lysosomes are a membrane bound cellular compartment containing proteases and dedicated to the degradation of proteins found in membranes or soluble proteins imported into the cell

53
Q

what is actin?

A

Actin - An example of sequestering proteins
regulating protein assembly and function

54
Q

Sequestration – The activities of proteins can be controlled by _____that _______. Another type of sequestration involves _____ – for example some transcription factors are held in the cytosol until signals cause modifications that allow their entry into the nucleus where they can function

A

sequestering proteins, bind and prevent assembly.

localization

55
Q

Many enzymatic reactions or pathways are
self-regulated by ___ mediated
by the end products

A

feedback inhibition

56
Q

True or False:Feedback inhibition typically occurs by enzymes sensing too much product for their reaction building up via a special regulatory site on the enzyme

A

True

57
Q

When a protein binds a ligand or another protein and this induces a conformational change that opens another binding site in the molecule this is known as:

A

allosterism

58
Q

An ____ change due to binding of a ligand that promotes the binding of a second ligand

A

allosteric

59
Q

Kinases _____ phosphate groups, which ____ substrate proteins.

A

add; activate or deactivate

60
Q

4 key mechanisms plus many others control protein activities:

A
  1. Modification by attachment of ubiquitin to lysine residues
  2. Modification by protein phosphorylation/dephosphorylation
    Occurs on polar non-charged residues – ser, thr, tyr
  3. Nucleotide binding and hydrolysis
  4. Modification by lipid anchor addition to C terminal Cys
  5. Other modifications include proteolytic processing, methylation, acetylation and glycosylation of specific amino acids in proteins, among many others.
61
Q

By modifying proteins, cells create_____

A

at least two potential states of activity for any modified protein.

62
Q

if the modification or ligand binding is
_____, as many are, the protein can run through many cycles of function

A

reversible

63
Q

Dynamics of the _____ are regulated by ____ and_____ through the cell cycle

A

nuclear lamins, phosphorylation and dephosphorylation

64
Q

Phosphatases _____ phosphate groups, which ____ substrate proteins

A

remove; activate or deactivate

65
Q

GTP hydrolysis inactivates

A

GTP-binding proteins

66
Q

Binding GTP activates

A

GTP-binding proteins

67
Q

“histone code”

A

methylation
phosphorylation
acetylation

68
Q

____ and _____ occur as
covalent modifications of _____

A

methylation, acetylation

basic amino acids

69
Q

***T/F : Phosphorylation of some substrates by protein phosphatases is typically reversible

A

False***