Brainscape's Knowledge GenomeTM

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


See full index

Biology > B1.2 Proteins > Flashcards

B1.2 Proteins Flashcards

1
Q

OH in condensation reaction comes from…

A

COOH Group

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

H comes from… in condensation reaction.

A

NH2 Group

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

Essential amino acids are..

A

Amino acids that cannot be synthesized by the body and must be obtained from diet.

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

How many essential amino acids are there?

A

9

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

Phenylaline is…

A

Essential

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

What determines the sequence of amino acids in a polypeptide?

A

The sequence of bases in the DNA of the gene it’s is coded for by.

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

How many polypeptides have been identified?

A

Over 2 million

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

What does heat do to proteins?

A

Causes vibrations that break intermolecular H bonds and cause their conformation to change

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

Half of R-Groups are

A

Hydrophobic, some with rings of atoms and one containing sulfur (methionine).

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

1st Third of Hydrophilic R-groups are

A
  • polar, but don’t ionize
  • Can form H bonds with other r-groups
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

2nd third of hydrophilic R-groups…

A

are basic as they have an amine group that can accept a proton

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

Final third of hydrophilic R-Groups…

A

are acidic because they can donate a proton and can form ionic bonds with positive R-Groups.

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

Pairs of R-groups that are mildly hydrophilic and contain a -SH group form:

A

a covalent S-S bond called a disulfide bond

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

Glycine has a

A

single hydrogen atom

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

Largest R-Group?

A

Tryptophan

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

Primary Structure

A

The number and sequence of amino acs in a polypeptide

17
Q

Carbon and changes in structure?

A

Due to bond rotation, alternative structures for the same compound can be formed.

18
Q

Each N in the repairing sequence of the polypeptide back bone has…

A

an H bonded to it

19
Q

Hydrogen bonds on secondary structures are formed between…

A

N-H groups and C=O groups

20
Q

Four types of interaction between amino acids in a tertiary structure:

A
  • Hydrogen bonds between polar R-groups
  • Ionic bonds between NH+ and COO- groups
  • S-S covalent bonds
  • Hydrophobic interactions between non-polar R-groups
21
Q

Proteins with ……… amino acids on their outer surface have …… amino acids at there core.

What does that do?

A
  • 1) Hydrophilic, Hydrophobic
  • Stabilizes protein’s tertiary structure in aqueous solutions.
22
Q

Some proteins have hydrophobic amino acids on their outer surface and are therefore attracted to the non-polar core of membranes, what does that make them?

A

Integral Membrane proteins

23
Q

What determines the tertiary structure of proteins and where they are located in cells?

A

The distribution of polar and non-polar amino acids.

24
Q

Water soluble protein are more likely to be located where in a cell?

A

Dissolved in cytoplasm or in aqueous solutions

25
Q

Proteins that contain a non-polypeptide structure known as a “prosthetic” group are called…

A

Conjugated Proteins

26
Q

Why is Hemoglobin a conjugated protein?

A

It contains haem groups which are not polypeptides.

27
Q

Quaternary structures?

A

Structures that contain two or more polypeptides linked to form a protein.

28
Q

What form feature of fibrous proteins gives them structural roles within and between cells?

A
  • Unfolded Polypeptides, which give them a narrow and elongated shape.
29
Q

Why do globular proteins have a rounded shape?

A

They have folded polypeptides

30
Q

Collagen is a ….. protein.

A

Fibrous

31
Q

What feature of collagen allows it to be wound together into a triple helix?

A

It has three polypeptides that are more elongated than then alpha helix.

32
Q

Form: Collagen has three polypeptides with an amino acid sequence that prevents the formation of an alpha helix.
What is the function?

A

This gives it a rope-like formation, it can withstand tensions by stretching rather than breaking, it’s released into extracellular matrix of tissues where tensile strength is needed. (Skin, bones, tendons, and ligaments.)

33
Q

Insulin is a ……. Protein

A

Globular

34
Q

Form: Insulin has a small size and a hydrophilic surface.
What is the function?

A

Allows insulin to be carried dissolved in blood plasma.

35
Q

Form: Insulin has a distinctive shape
Function?

A

Allows it to bind to a site on a specific receptor protein located in the plasma membrane of target cells.

36
Q

Insulin’s A-Chain has …… amino acids.

A

21

37
Q

Insulin’s chain has ……. amino acids.

A

30

Biology (20 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions