chapter 4 cell biology Flashcards

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1
Q

Proteins fold into ____ that represent_____ ______

A

conformations energy minima

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2
Q

Unfolded proteins are said to be

A

denatured

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3
Q

Molecular chaperones

A

in the cell help proteins

fold into their correct conformations

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4
Q

A protein’s structure will be determined by

A

its primary sequence.

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5
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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6
Q

peptide bond is _____ and

has no ______ in this region.

A

plannar rotation

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7
Q

Proteins can fold into many possible _______
however energetics drives them to ____ ____ ___
for each protein

A

conformations, one stable conformation

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8
Q

Folding starts co-translationally which means

A

chaperone proteins are needed

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9
Q

Proteins can often refold by themselves in _______

A

solution

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10
Q

____________ bonds serve to generate structure

in proteins. These can occur between _________ &______ backbone.

A

Weaker, non-covalent, R groups or parts of the polypeptide

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11
Q

__________________ also are key to specific

_______ binding of proteins. This occurs through the formation of ______ _______

A

Weaker, non-covalent bonds, ligand, binding sites.

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12
Q

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

A

non polar

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13
Q

Water interactions will often help to drive protein folding becuase

A

of its polar charge and the polar and non polar amino acids in proteins

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14
Q

A.a that are Charged residues are

A

acidic and basic)

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15
Q

A.a that Polar residues are are involved in

A

phosphorylation, glycosylation

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16
Q

(Ser, Thr, Tyr) are involved in

A

phosphorylation

17
Q

(Asn, Ser, Thr)

A

glycosylation

18
Q

Cysteine forms (3)

A

disulfide bridges)

intrapolypeptide, interpolypeptide

19
Q

______ in proteins are part of tertiary structure.

They are often arrangements of linked regions of ____ _____ & _____ _____

A

Domains alpha helices and beta sheets.

20
Q

________ ______ between domains can

provide a variety of functions.

A

Unstructured regions

21
Q

R groups locally

are hydrophobic, so ___ ____ may be favored

A

alpha helices

22
Q

alpha helices will tend to associate that region

of the protein into

A

membrane bilayers –

transmembrane domains

23
Q

coiled-coils are formed by

A

hydrophobic a.a twist in a sturucure and then twist together

24
Q

Beta sheets can have
either of two
arrangements

A

parallel or

anti-parallel

25
Q

______ can form ______ _______ bridges, which can

help stabilize protein structures in harsh environments.

A

Cysteines, covalent disulfide

26
Q

______ contain many intra- and inter-polypeptide _______ _______
that help maintain their conformations

A

Antibodies, disulfide bridges

27
Q

a single polypeptide (), two copies (), three ()

A

monomer, homodimer, homotrimer

28
Q

Some proteins can be mixed multimers containing different

A

subunits , eg AAB , ABC

29
Q

Proteins are organized into of _____ similar

sequence and conformation

A

families

30
Q

Hemoglobin is a _______ in which each subunit binds a ____ _____ which then binds an ____

A

heterotetramer, heme group oxygen

31
Q

examples of Non-protein components of proteins

A

heme (hemoglobin)

retinal (rhodopsin)

32
Q

A common theme in cells is dynamic assembly of ______

A

subunits

into a filament

33
Q

Ribozymes

A

Catalytic RNA molecules thatact as enzymes

34
Q

Prions (simple deff)

A

Proteinaceous Infectious Particles

35
Q

what are the Human Prion Diseases

A

Kuru
Creutzfeldt-Jakob disease
Gerstmann Straussler-Sheinker disease
Familial fatal insomnia

36
Q

Prion properties

A

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

37
Q

_____ ______ _____underlie prion formationand formation of _____ fibers

A

Protein conformation changes, amyloid

38
Q

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

A

template, PrP

39
Q

Spongiform encephalies

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