Week 2: Intro to Protein Structure Flashcards

1
Q

What are the levels of protein structure?

A

Primary > Secondary > Tertiary > Quaternary > Multiprotein complexes

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2
Q

Which levels of proteins do only SOME proteins have?

A

Quaternary and multiprotein complexes

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3
Q

What are proteins composed of?

A

Amino acids

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4
Q

What differentiates amino acids from each other?

A

The side-chain/R group

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5
Q

What are the major categories of amino acids?

A

Acidic, basic, uncharged polar, nonpolar

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6
Q

What are the parts of an amino acid?

A

Amino group, alpha carbon, carboxyl group, R-group

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7
Q

True or False: The grouping of genetic codes is perfect

A

False

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8
Q

What makes cysteine stand out?

A

Its ability to create disulfide bonds

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9
Q

Where are regular cysteine (no disulfide bonds) regularly found?

A

In reduction conditions in the cytosol

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10
Q

Where are the cysteine that form disulfide bonds regularly found?

A

In oxidation conditions in the ER outside the cell

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11
Q

What is an important property of disulfide bonds?

A

They have strong covalent bonds

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12
Q

Disulfide bonds act as braces, which helps to hold the _________ in proper configuration

A

Protein shape

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13
Q

What kind of bond holds amino acids together?

A

Peptide bond

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14
Q

What are examples of more proper names for the components of an amino acid, post-peptide bond?

A

R-group + main parts = reisdue
Carboxyl carbon = carboNYL carbon
Amino group nitrogen = amiDE nitrogen

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15
Q

What happens when a peptide bond forms (besides the joining of two amino acids)? What kind of reaction is this?

A

The OH from one AA’s carboxyl group and the hydrogen from another AA’s amino group make water. This is a condensation reaction

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16
Q

What is considered a polypeptide chain?

A

2 or more AA together

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17
Q

What is lies at the end of polypeptide chains?

A

An amino end (N-terminus) and Carboxyl end (C-terminus)

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18
Q

True or False: Differences in primary AA sequence DO NOT matter

A

False

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19
Q

True or False: The order of AA acids are important

20
Q

How many residues do you need to create an alpha helix?

A

> 4 residues

21
Q

What properties differentiate alpha-helices from DNA double-helices?

A

Alpha-helix:
- R-groups OUTWARD
- R-groups DO NOT hold it together (No H-bonds)
- SINGLE strand
- N-end, C-end

DNA double helix:
- Base pairs face INWARDS
- Base pairs HELP hold it together
- DOUBLE strand
- Anti-parallel

22
Q

What bonds stabilizes the beta sheet?

A

H-bonding between carbonyl oxygen (C=O) of 1 AA and amide hydrogen (N-H) of AA in NEIGHBOURING strand

23
Q

True or False: R groups are involved in the stability of beta sheets

24
Q

What are the two types of beta sheets?

A

Anti-parallel and parallel

25
Q

What is the difference between the two types of beta sheets?

A

Anti-parallel face the opposite directions while parallel face the same directions

26
Q

True or False: A coiled coil is a tertiary protein structure

A

False!!!!!!!!

27
Q

What does it mean when an alpha helix is amphipathic?

A

Two different biochemical/biophysical properties on two different sides. One side is hydrophobic while the other is hydrophilic.

28
Q

Where can coiled coils be found?

A

alpha-keratin of skin, hair, and myosin motor proteins

29
Q

Why does the hydrophobic strand coil inwards?

A

There is H2O all around the cell, the hydrophobic strand coils inward to get away from the water.

30
Q

What is the tertiary structure of a protein?

A

The overall 3D structure of the protein

31
Q

What is the tertiary structure of a protein held together by?

A

Hydrophobic bonds, non-covalent bonds, covalent disulfide bonds

32
Q

Proteins generally fold into the conformation that is the most __________ _________

A

energetically favourable

33
Q

Proteins will fold into the shape dictated by their amino acid sequence. What makes this process more efficient and reliable in living cells?

A

Chaperone proteins

34
Q

What are protein domains in tertiary structures?

A

Domains are portions of a protein that has its OWN tertiary structure, often functioning in a SEMI-INDEPENDENT manner

35
Q

Eukaryotic proteins often have 2 or more domains connected by ___________ ____________ ____________

A

intrinsically disordered sequences

36
Q

True or False: Connectors are not really part of the domain

37
Q

What makes protein families alike?

A

Similar sequences and tertiary structures

38
Q

What makes protein families different?

A

They often evolve to have different structures

39
Q

What subunits make up the hemoglobin protein?

A

2 alpha helices, 2 beta sheets

40
Q

True or False: 1 polypeptide chain can make up one protein

41
Q

What makes up multiprotein complexes & molecular machines?

A

Many identical subunits, mixtures of different proteins and DNA/RNA, and very dynamic assemblies of proteins to form molecular machines

42
Q

What are examples of multiprotein complexes & molecular machines?

A

Actin filaments, viruses and ribosomes, machines for DNA replication initiation or for transcription

43
Q

What are the steps for studying a single or a few proteins?

A
  1. Purify protein or proteins of interest (i.e. various types of electrophoresis & affinity chromatography
  2. Determine amino acid sequences (e.g. Mass spectrometry)
  3. Discover precise 3D structure using techniques such as: x-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, or cry-electron microscopy and other techniques
44
Q

What is proteomics?

A

Large scale study of proteins

45
Q

Researchers usually use a range of “____-____” and computational approaches to collect & analyze data on the set of proteins in a sample

46
Q

What are some examples of the types of data of analyses performed?

A
  • Protein-protein interactions, regulation of these interactions, & their position within a pathway
  • Abundance & turnover to protein
  • Location within a cell or tissue
  • Bioinformatics, statistics, & artificial intelligence (e.g. machine-learning-based algorithms), often in combination with other “omics” data sets