Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Cell, Organisms And Systems > Protein Structure and Function > Flashcards

Protein Structure and Function Flashcards

1
Q

Covalent bonds

A

Join building blocks into macromolecules like DNA.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Non-covalent bonds

A

Stabilize macromolecule shapes crucial for cellular life.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Macromolecules

A

Large biological molecules like proteins and nucleic acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Dehydration reactions

A

Join monomers by removing water, forming polymers.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

ATP

A

Energy currency of the cell, vital for metabolism.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Redox reactions

A

Chemical reactions involving electron transfer, essential for life.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Amino acids

A

Building blocks of proteins, linked by peptide bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Peptide bonds

A

Link amino acids, formed by dehydration reactions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Protein structure levels

A

Include primary, secondary, tertiary, and quaternary structures.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Globular proteins

A

Compact proteins, often soluble, with diverse functions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Fibrous proteins

A

Structural proteins, elongated and insoluble in water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Protein misfolding

A

Incorrect folding can lead to diseases like Alzheimer’s.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Protein-protein interactions

A

Crucial for biological processes and cellular functions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

N-terminal

A

Free amino end of a polypeptide chain.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

C-terminal

A

Free carboxyl end of a polypeptide chain.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Zwitterions

A

Amino acids at physiological pH with no net charge.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Chirality

A

Property of amino acids, except glycine, having two forms.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Hydrophobic amino acids

A

Tend to be inside globular proteins, avoiding water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Hydrophilic amino acids

A

Able to form hydrogen bonds, found on protein surfaces.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Disulfide bonds

A

Covalent bonds formed between cysteine residues.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Secondary structure

A

3D structure formed by hydrogen bonds in polypeptides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Alpha helix

A

Tightly coiled structure with R groups projecting outward.

23
Q

Beta sheets

A

Formed by adjacent strands linked by hydrogen bonds.

24
Q

Random coil

A

Irregular arrangement of polypeptide chains.

25
Q

Motifs

A

Specific arrangements of secondary structure elements.

26
Q

Leucine zipper

A

Example of an alpha helical protein involved in gene regulation.

27
Q

Fibroin

A

Silk protein with antiparallel beta sheet structure.

28
Q

Hydrogen bonding

A

Interactions stabilizing secondary protein structures.

29
Q

Tertiary structure

A

Overall 3D arrangement of protein atoms.

30
Q

Native fold

A

Specific conformation enabling biological function.

31
Q

Cystine

A

Dimer of cysteine linked by disulfide bond.

32
Q

Insulin

A

Hormone stored as inactive hexamer, active as monomer.

33
Q

Protein domains

A

Independently stable structural motifs in proteins.

34
Q

Kinase domain

A

Common protein domain involved in phosphorylation.

35
Q

Quaternary structure

A

Association of multiple polypeptide chains.

36
Q

Homo-multimers

A

Complexes of identical polypeptide chains.

37
Q

Hetero-multimers

A

Complexes of different polypeptide chains.

38
Q

Primary structure

A

Linear sequence of amino acids in a protein.

39
Q

Protein diversity

A

Variety of protein structures reflecting function.

40
Q

α-Keratin

A

Coiled-coil fibrous protein providing structural support.

41
Q

Membrane proteins

A

Proteins interacting with lipid bilayers.

42
Q

G-protein-coupled receptors (GPCRs)

A

Large family of membrane proteins with seven domains.

43
Q

Ligand

A

Small molecule that binds to a protein.

44
Q

Induced fit model

A

Conformational change upon ligand binding.

45
Q

Enzymes

A

Proteins that catalyze biochemical reactions.

46
Q

Active site

A

Region where substrate binds on an enzyme.

47
Q

Transition state

A

Intermediate state during a chemical reaction.

48
Q

Inhibitors

A

Molecules that decrease enzyme activity.

49
Q

Peptidoglycan

A

Structural component of bacterial cell walls.

50
Q

Penicillin

A

Antibiotic that irreversibly inhibits transpeptidase.

51
Q

Neurodegenerative diseases

A

Diseases linked to protein misfolding and aggregation.

52
Q

Lewy bodies

A

Intraneuronal aggregates associated with Parkinson’s disease.

53
Q

Alpha-synuclein

A

Protein linked to Lewy bodies in Parkinson’s.

Cell, Organisms And Systems (17 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions