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CHEM 123 > P3.2. Protein > Flashcards

P3.2. Protein Flashcards

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1
Q
  • naturally-occurring
  • unbranched polymer in which the monomer units are amino acids
A

PROTEIN

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2
Q

Elemental Compositon of Protein:

A

Carbon
Hydrogen
Oxygen
Nitrogen
may also contain Sulfur

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3
Q

average nitrogen content of proteins

A

15.4% by mass

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4
Q

Some elemental composition that can be present in proteins are:

A

Fe, P, and some other metals in some specialized protein

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5
Q

a peptide in which at least 40 amino acid residues are present

A

PROTEIN

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6
Q

Several proteins with ____ amino acid residues are known

A

GREATER THAN 10,000

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7
Q

Common proteins contain ____ amino acid residues

A

400–500

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8
Q

Small proteins contain ____ amino acid residues

A

40–100

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9
Q

TRUE OR FALSE?

There can be more than one peptide chain may be present in a protein.

A

TRUE

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10
Q

contains one peptide chain

A

monomeric protein

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11
Q

contains more than one peptide chain

A

multimeric protein

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12
Q

2 PROTEIN CLASSIFICATION BASED ON CHEMICAL COMPOSITION:

A

Simple Proteins
Conjugated Proteins

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13
Q
  • only amino acid residues are present.
  • more than one protein MAY BE PRESENT, but ALL SUBUNITS contain only AMINO ACIDS.

protein portion - AMINO ACIDS

A

Simple Proteins

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14
Q

A protein that has one or more non-amino acid entities (prosthetic groups) present in its structure

A

Conjugated Protein

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15
Q
  1. non-amino acid entities are ____.
  2. non-amino acids components may be ____.
A
  1. prosthetic groups
  2. organic/inorganic - prosthetic groups
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16
Q

Examples of Prosthetic Groups:

A
  • Lipoproteins
  • Glycoproteins
  • Metalloproteins
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17
Q

TRUE OR FALSE?
One or more polypeptide chains may be present in Conjugated Proteins.

A

TRUE

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18
Q

TRUE OR FALSE

Non-amino acid components in Conjugated protein may be organic or inorganic prosthetic groups.

A

TRUE

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19
Q

contain lipid prosthetic groups

A

Lipoproteins

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20
Q

contain carbohydrate groups

A

Glycoproteins

21
Q

contain a specific metal as prosthetic group

A

Metalloproteins

22
Q

Four types of Protein Structures:

A
  • PRIMARY STRUCTURE
  • SECONDARY STRUCTURE
  • TERTIARY STRUCTURE
  • QUATERNANRY STRUCTURE

these four dictates the function & defines the morphology of proteins

23
Q

refers to the order [number and sequence] in which amino acids are linked together in a protein

A

PRIMARY STRUCTURE OF PROTEINS

24
Q

the number and sequence of amino acids linked by the amides/peptide bonds are dictated by?

A

DNA CODING

25
Q

sequenced and determined the primary structure for the first protein hormone - Insulin

its:
- molecular structure
- identity
- binding capacity/ability

A

Frederick Sanger (1953)

26
Q
  • interaction of adjacent amino acids

its 3 forms?

A

SECONDARY STRUCTURE OF PROTEINS

  1. alpha-helix [spring]
  2. beta-pleated [corugated form]
  3. random [without pattern]
27
Q

The peptide linkages [in SECONDARY STRUCTURE of Proteins] are essentially ____ thus allows only two possible arrangements for the peptide backbone

A

planar

28
Q

The peptide linkages [in SECONDARY STRUCTURE of Proteins] are essentially planar thus allows only two possible arrangements for the peptide backbone…

ITS REASONS:

A
  • For two amino acids linked through a peptide bond six atoms lie in the same plane
  • The planar peptide linkage structure has considerable rigidity, therefore rotation of groups about the C–N bond is hindered
  • Cis–trans isomerism is possible about C–N bond.
  • The trans isomer is the preferred orientation

yung naka-bold lang tandaan HAHAHAHA. Explain in own words na langs~

29
Q
  • single protein chain
  • shape: COILED SPRING [HELIX]
  • coiled helical spring
  • its R-group are outside the Helix because there is not enough room for them to stay inside.
  • H-bonding between same amino acid chains – INTRAMOLECULAR

SAME AMINO ACIDS - HYDROGEN BONDING

R-GROUP OUTSIDE!!!

A

Alpha-helix (a-helix)

30
Q
  • Completely extended amino acid chains
  • Side chains below or above the axis
  • H-bonding between two different chains – INTER or/and INTRAMOLECULAR

DIFFERENT AMINO ACIDS - HYDROGEN BONDING

R-GROUP/SIDE CHAINS - TOP OR BOTTOM!!!

A

Beta-pleated sheets (b-pleated sheet)

31
Q
  • overall three-dimensional shape of a protein
  • interactions between amino acid side chains (R groups) that are widely separated from each other
  • defines the physical & chemical properties of proteins
A

TERTIARY STRUCTURE OF PROTEINS

32
Q

4 types of interactions are observed in Tertiary Structure of Proteins:

A
  1. Disulfide Bond
  2. Electrostatic Interactions
  3. H-bondings
  4. Hydrophobic interactions
33
Q
  • covalent
  • strong
  • between two cysteine groups
A

Disulfide Bond

34
Q
  • Salt Bridge between charged side chains of acidic and basic amino acids
A

Electrostatic Interactions

-OH
-NH2
-COOH
-CONH2

35
Q
  • bonding between polar, acidic and/or basic R groups
  • for this bonding to occur, it must be attach to what elements?
A
  1. H-bonding (Hydrogen Bonding)
  2. OXYGEN, NITROGEN, FLUORINE
36
Q

interaction between non-polar side chains.

A

Hydrophobic Interactions

37
Q
  • HIGHEST level of protein organization.
  • 2 or more chains/subunits attract to form proteins.
A

QUATERNARY STRUCTURE OF PROTEINS

38
Q

Most ____ contain an even number of subunits (two subunits a dimer, four subunits a tetramer, and so on).

A

multimeric proteins

39
Q

held together mainly by hydrophobic interactions between amino acid R groups.

A

subunits

40
Q
  • example of a protein with quaternary structure.
  • oxygen carrying protein in blood
  • tetramer in which there are two identical a chains and two identical B chains

Each chain in this protein enfolds a ____, the site where oxygen binds to the protein.

A

Hemoglobin

heme group

41
Q

Proteins Classification based on SHAPE:

A
  1. FIBROUS PROTEINS: Collagen
  2. GLOBULAR PROTEINS: Myoglobin & Hemoglobin
42
Q
  • Most abundant proteins in humans (30% of total body protein)
  • Major structural material in CONNECTIVE TISSUES [tendons, ligaments, blood vessles, skin]
  • Organic component of bones and teeth
  • Predominant structure - TRIPLE HELIX
  • Rich in proline (up to 20%) – important to maintain structure
A

COLLAGEN

43
Q

Collagen is rich in what derivatives?

A

4-hydroxyproline (5%)
5-hydroxylysine (1%)

44
Q

some hydroxylysines are linked to ____ and ____, and their ____ that helps in aggregation of collagen fibrils.

aggregation: cluster

A
  1. glucose
  2. galactose
  3. disaccharides
45
Q
  • oxygen storage molecule in muscles.
  • Monomer - single peptide chain with one heme unit
  • Binds one O2 molecule
  • oxygen serves as a reserve oxygen source for working muscles
A

Myoglobin

46
Q

TRUE or FALSE:
myglobin has a higher affinity for oxygen than hemoglobin.

A

TRUE

47
Q
  • An oxygen carrier molecule in blood
  • Transports oxygen from lungs to tissues
  • Tetramer (four peptide chains) - each subunit has a heme group
  • Can transport up to 4 oxygen molecules at time

Iron atom in heme interacts w/…

A

Hemoglobin

Oxygen

48
Q

PROTEINS CLASSIFICATION BASED ON FUNCTION:

A
  1. ability to bind small molecules
  2. ability to bind other proteins
  3. ability integrated into cell membranes

Proteins is the most versatile macromolecule.

CHEM 123 (46 decks)

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