Brainscape's Knowledge GenomeTM

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


See full index

CHEM 2N LECTURE > PROTEINS PT.2 > Flashcards

PROTEINS PT.2 Flashcards

You may prefer our related Brainscape-certified flashcards:
Periodic Table flashcards Chemistry 101 flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

Specialized proteins involved in defending the body from antigens.

  • One way ____________ counteract antigens is by immobilizing them so they can be destroyed by white blood cells.
A

ANTI - BODIES

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

are responsible for muscle contraction and movement.

  • Examples of these proteins include actin and myosin.
  • As myosin and actin interact in the presence of ATP, they form a tight compact.
A

CONTRACTILE PROTEIN

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

Are proteins that facilitate biochemical reactions.

They are often referred to as catalysts, because they speed up chemical reactions.

A

ENZYMES

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

myosin and actin interact in the presence

A

ATP

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

CHARACTERISTICS OF PROTEINS

A
  1. Can be broken down into separate units by the use of enzyme.
  2. Consist of amino group and acid group (ampotheric).
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Are messenger proteins which help to coordinate certain bodily activities.

A

HORMONAL PROTEINS

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

examples of hormonal proteins

A

INSULIN, OXYTOCIN, SOMATOTROPHIN

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

FUNCTIONS OF PROTEINS

A

 Antibodies
 Contractile proteins
 Enzymes
 Hormonal proteins
 Structural proteins
 Storage proteins
 Transport proteins

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

regulates glucose metabolism by controlling the blood-sugar concentration.

A

INSULIN

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

stimulates contractions during childbirth.

A

OXYTOCIN

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

Are fibrous and stringy and
because of this formation, they provide support for
various body parts.

A

STRUCTURAL PROTEINS

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

is a growth hormone that stimulates protein
production in muscle cells.

A

SOMATOTROPHIN

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

EXAMPLE OF STRUCTURAL PROTEINS

A

KERATIN, COLLAGEN, ELASTIN

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

strengthen protective coverings such as skin, hair, quills, feathers, horns, and beaks.

A

KERATIN

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

provide support for connective tissues such as tendons and ligaments.

A

COLLAGEN & ELASTIN

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

basic structural building blocks of protein.

 molecules having one amino group , one carboxyl group, one H atom and one specific
group (R group) attached to the central C atom.

A

AMINO ACIDS

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

store amino acids for the body to use later.

A

STORAGE PROTEIN

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

another protein that stores iron in the transport protein, hemoglobin.

A

FERRITIN

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

which move molecules from one place to another around the body.

A

CARRIER PROTEINS

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

is one of these and is responsible for transporting oxygen through the blood via red blood cells.

A

HEMOGLOBIN

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

proteins are “_________”

A

UNIQUE

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

Contains C, H, O, N

 Has both hydrophobic & hydrophylic ends.

 Makes polypeptide then makes proteins

 Differ in R-group

 R-group can be acidic, basic or neutral

A

AMINO ACIDS MONOMER

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

are another that operate in the electron transport chain as electron carrier proteins.

A

CYTOCHROMES

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

EXAMPLES OF PROTEIN RICH FOOD

A
  1. Lean white meats
  2. Soy
  3. Beef
  4. Beans
  5. Eggs
  6. Dairy
  7. Seafood
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

NON - POLAR AMINO ACID

A

Glycine, Alanine, Valine, Leucine, Isoleucine, Proline, Phenylalanine, Methionine, Tryptophan

17
Q

POLAR NEUTRAL AMINO ACID

A

Serine, Cysteine, Threonine, Asparagine, Glutamine, Tyrosine

18
Q

POLAR ACIDIC AMINO ACID

A

Asparatic acid and Glutamic acid

19
Q

POLAR BASIC AMINO ACID

A

Histidine, Lysine and Arginine

20
Q

an amino acid that
contains one amino group,one carboxyl group,and nonpolar side chain.

  • When incorporated into a protein,such amino acids are hydrophobic(water-fearing).
A

NON - POLAR AMINO ACID

20
Q

an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral (neither acidic nor basic).

A

POLAR NEUTRAL AMINO ACID

20
Q

R-group can be ____, _____, OR ________

A

ACIDIC, BASIC, NEUTRAL

20
Q

an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain.

A

POLAR ACIDIC AMINO ACID

21
Q

an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain.

A

POLAR BASIC AMINO ACID

21
Q
  • Have straight side chains.
  • (threonine, glycine, serine, alanine)
A

ALIPHATIC AA’s

22
Q

Those that contain additional acidic or basic
group classified into:

A

A. Aliphatic AAs
B. Aromatic or cyclic AAs.

23
Q
  • Contain a ring structure
  • (tryptophan, phenylalanine, tyrosine)
A

AROMATIC OR CYCLIC AA’s

24
Q
  • those with additional amino acid group.
  • (Lysine, Arginine, Histidine)
A

BASIC AA’s

25
Q

Those that contain additional carboxyl group.
 (aspartic acid, glutamic acid)

A

ACIDIC AA’s

26
Q

are AAs having aliphatic side- chains with a branch
( a carbon atom bound to more than two other carbon atoms.)

A

Branched- chain amino acids (BCAA)

27
Q

There are _____________ used by the ribosomes to make proteins.

A

20 common α-amino acids

28
Q

are used clinically to aid in the recovery of burn patients, and supplementation of strength athletes.

A

BRANCHED - CHAIN AMINO ACIDS (BCAA)

29
Q

EXAMPLES OF BCAA

A

(leucine, isoleucine, valine)

30
Q

CLASSIFICATIONS OF AMINO ACID

A

 According to the structure of side chain.
 According to polarity of the side chain
(R group)
 According to the nutritional requirements
 According to the metabolic fate

30
Q

Glutamate from ____________.

A

wheat gluten

31
Q

Greek word of Tyrosine from cheese

A

“TYROS”

32
Q

cannot be synthesized itself by the organism
(usually referring to humans), and therefore must be supplied in the diet.

A

ESSENTIAL AMINO ACID

33
Q

help the body function andregulate neurotransmitters, chemicals in the brainthat control mood and behavior.

A

ESSENTIAL AMINO ACID

34
Q

are generally compact, soluble, and more/less spherical to oblate or egg-shaped.

A

GLOBULAR PROTEINS

35
Q

ALBUMIN IN ____

A

EGG

36
Q

CASEIN IN _______ & ______

A

MILK AND CHEESE

37
Q

are typically elongated and insoluble.
Long coiled or folded chains of amino acids bound together in parallel line.

A

FIBROUS PROTEINS

37
Q

GLOBULIN IN ______

A

RED BLOOD CELLS

38
Q

hey are able to provide support for cells and tissues

A

FIBROUS PROTEINS

38
Q

can be synthesized by adults but not by growingchildren, hence these are considered as semiessential amino acids.

A

SEMI - ESSENTIAL AMINO ACID

39
Q

EXAMPLE OF ESSENTIAL PROTEIN

A
  • Tryptophan
  • Valine
  • Threonine
  • Isoleucine
  • Leucine
  • Lysine
  • Phenylalanine
  • Methionine
40
Q
  • These can be synthesized by the body to meet the biological needs.
  • need not to be consumed through the diet.
A

NON - ESSENTIAL AMINO ACID

41
Q

refers to highly regular
local sub-structures.

  • Extended conformation of polypeptide chains
A

SECONDARY STRUCTURE

41
Q
  • Linear arrangement of amino acids present in the polypeptide chain.
  • Each protein has a distinctive number and sequence of amino acid residues
A

PRIMARY STRUCTURE

41
Q

HEMOGLOBIN

A

QUARTERNARY STRUCTURE

41
Q

refers to three dimensional structure of a single protein molecule.

Connectivity between two (or) more polypeptide chain.
* These chains may be identical (or) different in primary structure.

A

TERTIARY STRUCTURE

42
Q
A

CHEM 2N LECTURE (4 decks)

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