1.3 - INTRODUCTION TO MOLECULAR BIOLOGY Flashcards

1
Q

✓ All newly synthesized proteins need to fold up correctly (3-D shape)
* Native conformation
* Non-native (e.g., unfolded or misfolded)
* Essential for enzymatic activity or structural roles in the cell

A

Post-translational modifications
(PTMs)

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2
Q

stabilize partially folded
regions in their correct form

A

Chaperone proteins

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3
Q

Proteins fold in the

A

ER

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4
Q

✓ Amino acids of some proteins need to be chemically modified
* Addition of phosphate groups
* Phosphorylation can determine protein function

A

Post-translational modifications
(PTMs)

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5
Q

increase the functional diversity of the proteome by the covalent addition of functional groups, proteolytic cleavage of regulatory subunits, or degradation of entire proteins

A

Post-translational modifications (PTMs)

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6
Q

PTMs include ?; influence almost all aspects of normal cell biology and pathogenesis

A

phosphorylation, methylation and acetylation

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7
Q

Identifying and understanding PTMs is critical in the study of ?

A

cell biology and disease treatment and prevention

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8
Q

most common mechanism of regulating protein function and transmitting signals throughout the cell. Protein phosphorylation (e.g., serine, threonine, or tyrosine residue) is one of the most important and well-studied PTMs.

A

Phosphorylation

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9
Q

refers to addition of a methyl group to lysine (K) or arginine (R) residue of a protein. Methylation is mediated by methyltransferases and S-adenosyl methionine (SAM) is the primary methyl group donor

A

Methylation

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10
Q

refers to the addition of acetyl group in a protein. It is catalyzed by histone acetyltransferase (HAT) that transfer the acetyl moiety from acetyl-CoA to the amino group of lysine (K) residue

A

Acetylation

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11
Q

Conformation of a Protein

A

Primary
Secondary
Tertiary
Quaternary

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12
Q

amino acid sequence in a polypeptide chain

A

Primary

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13
Q

loops, coils, barrels, helices, sheets, or other shapes formed by hydrogen bonds between neighboring carboxyl and amino groups

A

Secondary

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14
Q

three-dimensional forms shaped by bonds between R groups, interactions between R groups and water

A

Tertiary

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15
Q

protein complexes formed by bonds between separate polypeptides

A

Quaternary

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16
Q

Proteins must fold into ? to function

A

1 or more specific shape(s) or conformation(s)

17
Q

The 3-D conformation determines a

A

protein’s function

18
Q

Folding occurs because of

A

attractions and repulsions between atoms

19
Q

Some amino acids are attracted to water

A

hydrophilic

20
Q

Repelled water

A

hydrophobic

21
Q

Misfolded Protein in Alzheimer

A

Amyloid beta precursor protein

22
Q

Alzheimer OMIM

A

104760

23
Q

Misfolded Protein Sclerosis

A

Superoxide dismutase

24
Q

Sclerosis OMIM

A

147450

25
Q

Huntington Misfolded Protein

A

Huntingtin

26
Q

Huntington OMIM

A

143100

27
Q

Parkinson Misfolded Protein

A

Alpha synuclein

28
Q

Parkinson OMIM

A

163890

29
Q

Prion disorders Misfolded Protein

A

Prion protein

30
Q

Prion disorders OMIM

A

176640

31
Q

OMIM

A

Online Mendelian Inheritance in Man