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BIOMOLECULAR > STRUCTURE AND F(X) OF AMINO ACIDS, PEPTIDES, AND PROTEINS > Flashcards

STRUCTURE AND F(X) OF AMINO ACIDS, PEPTIDES, AND PROTEINS Flashcards

1
Q

___ AND ___ ARE THE FUNCTIONAL GRP OF AMINO ACIDS.

A
  1. AMINO GRP
  2. CARBOXYL GRP
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2
Q

R GRP WILL DETERMINE THE ___ AND ___ OF AN AMINO ACID

A
  1. STRUCTURE
  2. PROPERTIES
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3
Q

STATE THE PROPERTIES OF AMINO ACIDS.

A
  1. STEREOISOMERS
  2. AMPHOTERIC
  3. HAS ITS OWN PK VALUE
  4. EXIST AS ZWITTERION
  5. HAS ITS OWN ISOELECTRIC POINT
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4
Q

WHAT IS MEANT BY AMPHOTERIC?

A
  • IT CAN EXIST AS BOTH ACID AND BASE
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5
Q

PROTEIN USUALLY ARE (D/L) ISOMERS

A

L ISOMERS

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6
Q

STATE THE CHARACTERISTICS OF NON POLAR SIDE CHAIN.

A
  1. IT IS DIVIDED INTO 2 WHICH ARE:
    - ALIPATHIC (GLYCINE, ALANINE, VALINE, LEUCINE, ISOLEUCINE)
    - AROMATIC (PHENYLALANINE, TYROSINE, TRYTOPHAN)
  2. IT DOES NOT FORM A HYDROGEN BOND
  3. IT PROMOTES THE HYDROPHOBIC INTERACTION - STABALISING THE PROTEIN STRUCTURE
  4. IT DOES NOT BIND OR DONATE PROTON/ PARTICIPATE IN HYDROGEN OR IONIC BOND.
  5. LOCATION: ON SURFACE OF MEMBRANE PROTEIN, INTERACT WITH THE LIPIDS
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7
Q

STATE THE CHARACTERISTICS OF POLAR UNCHARGED SIDE CHAIN.

A

POLAR UNCHARGED SIDE CHAIN:
1. EXAMPLE: THREONINE, CYSTEINE, SERINE
2. PROMOTE HYDROPHILIC INTERACTION: ZERO UNCHARGED AT NEUTRAL PH
3. CONTAIN:
- POLAR OH GRP: PARTICIPATE IN THE HYDROGEN BOND WITH WATER
- SH GRP: PARTICIPATE IN THE DISULFIDE BOND
4. LOCATTION: INTERIOR OF MEMBRANE ASSOCIATED PROTEINS

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8
Q

STATE THE CHARACTERISTIC OF ACIDIC SIDE CHAIN.

A

ACIDIC SIDE CHAIN:
- NEGAIVELY CHARGED
- IT CONTAINS THE CARBOXYLATE GRP
- IT IS A PROTON DONNOR
- EXAMPLE: ASPARTATE AND GLUTAMATE
- LOCATION: INTERIOR MEMBRANE OF ASSOCIATED PROTEIN

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9
Q

STATE THE CHARACTERISTICS OF BASIC SIDE CHAIN.

A

BASIC SIDE CHAIN
- POSITIVELY CHARGED
- IT CONTAINS THE AMINO GRPS.
- IT IS A PROTON ACCEPTOR
- EXAMPLE: LYSINE, ARGININE, HISTIDINE
- LOCATION: INTERIOR MEMBRANE OF ASSOCIATED PROTEIN

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10
Q

STATE THE AMINO ACID THAT HAVE NON POLAR SIDE CHAIN.

A

AROMATIC GRP:
1. PHENYLALANINE
2. TYROSINE
3. TRYTOPHAN
ALIPATHIC GRP:
1. GLYCINE
2. ALANINE
3. VALINE
4. LEUCINE
5. ISOLEUCINE

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11
Q

STATE THE AMINO ACID THAT HAVE POLAR UNCHARGED SIDE CHAIN.

A
  1. THREONINE
  2. CYSTEINE
  3. SERINE
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12
Q

STATE THE AMINO ACID THAT HAVE ACIDIC SIDE CHAIN.

A
  1. GLUTAMATE
  2. ASPARTATE
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13
Q

STATE THE AMINO ACID THAT HAVE BASIC SIDE CHAIN.

A
  1. LYSINE
  2. ARGININE
  3. HISTIDINE
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14
Q

STATE THE CLASSIFICATION OF AMINO ACID BASED ON ITS SIDE CHAIN

A
  1. POLAR UNCHARGED SIDE CHAIN
  2. NON POLAR SIDE CHAIN
  3. ACIDIC SIDE CHAIN
  4. BASIC SIDE CHAIN
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15
Q

STATE THE CHARACTERISTICS OF PRIMARY STRUCTURE OF PROTEINS.

A

PRIMARY STRUCTURE OF PROTEINS:
- IT IS CONNECTED BY THE PEPTIDE BONE
- IT IS A LINEAR SEQUENCE
- ITS SEQUENCE IS DETERMINE DURING THE DNA REPLICATION
- ALTERATION IN THE PRIMARY STRUCTURE CAN AFFECT THE PROTEIN’S FUNCTION AS WELL AS ITS CONFORMATION.

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16
Q

STATE THE CHARACTERISTICS OF SECONDARY STRUCTURE OF PROTEIN.

A

SECONDARY STRUCTURE OF PROTEINS:
- IT IS CONNECTED BY THE HYDROGEN BOND AT ITS REGULAR INTERVAL ALONG THE POLYPEPTIDE BACKBONE
- POLYPEPTIDE CHAIN CAN FOLD INTO;
1. COIL FORMING ALPHA HELIX: THE HYDROGEN BOND IS FORMED IN BETWEEN THE NH GRP AND CO GRP ON THE SAME STRAND. THE A HELIX WILL COIL AT EVERY 4TH AMINO ACID.
2. LIES PARALLEL TO EACH OTHER FORMING THE BETA PLEATED SHEET: THE HYDROGEN BOND IS FORMED IN BETWEEN THE AMINO GRP AND CARBON GRP ON THE ADJACENT STRAND.

17
Q

STATE THE CHARACTERISTICS OF TERTIARY STRUCTURE OF PROTEIN.

A

TERTIARY STRUCTURE OF PROTEIN:
- HELICAL FORM COILED INTO A BALL LIKE STRUCTURE TO PRODUCE THE 3D PROTEIN STRUCTURE
- THE FUNCTIONAL UNIT ARE CALLED AS DOMAIN
- THE FOLDING OF A PROTEIN INTO ITS DOMAIN RELATED TO THE HYDROPHOBIC AND HYDROPHILIC PROPERTIES OF AN AMINO ACIDS
- EXAMPLE: MYOGLOBIN
- TERTIARY STRUCTURE ARE HELD BY:
1. VAN DER WAALS INTERACTION
2. HYDROPHOBIC INTERACTION
3. HYDROGEN BOND
4. IONIC BOND
5. DISULPHIDE LINKAGE

18
Q

DESC THE TERTIARY STRUCTURE IN MYOGLOBIN.

A
  • MYOGLOBIN IS A TERTIARY STRUCTURE OF PROTEIN.
  • IT CONSIST OF A SINGLE POLYPEPTIDE CHAIN THAT FORM INTO SEVERAL ALPHA HELICAL FOILED INTO A 3D STRUCTURE.
  • MYOGLOBIN CONSIST ABOUT 154 AA.
  • IT WILL ATTACH TO HAEMOGLOBIN
  • THE FUNCTION OF MYOGLOBIN IS TO STORE THE OXYGEN IN MUSCLES.
19
Q

DESC THE CHARACTERISTICS OF QUATERNARY STRUCTURE.

A
  • QUATERNARY STRUCTURE CONSIST OF MORE THAN ONE BALL LIKE GLOBULAR PROTEIN THAT IS HELD BY WEAK INTERACTION.
  • 2 OR MORE POLYPEPTIDES JOIN IN THE AGGREGATION TO FORM THE QUATERNARY STRUCTURE.
  • EXAMPLE: HAEMOGLOBIN, DNA POLYMERASE
  • OFTEN, QUATERNARY STRUCTURE ARE COMPLEXED WITH DIFFERENT MOLECULE - SUCH AS HAEMOGLOBIN THAT CONSIST OF IRON
20
Q

COMPARE HAEMOGLOBIN AND MYOGLOBIN.

A

MYOGLOBIN:
1. IT CAN BE FOUND IN THE HEART AND SKELETAL MUSCLE.
2. IT IS A TERTIARY STRUCTURE
3. IT CAN BIND TO ONLY ONE OXYGEN AS IT HAS ONLY ONE HEME GRP.
4. IT ACTS AS A RESERVOIR FOR OXYGEN AND INCREASE THE RATE OF TRANSPORTATION OF OXYGEN WITHIN THE MUSCLE CELL

HAEMOGLOBIN:
1. IT CAN BE FOUND IN THE RED BLOOD CELL
2. IT IS A QUATERNARY STRUCTURE
3. IT CAN BIND TO 4 OXYGEN AS IT CONSIST OF 4 HEME GRPS
4. IT WILL TRANSPORT THE OXYGEN FROM THE LUNGS TO ALL CAPILLARIES OF TISSUES.

21
Q

STATE THE CHARACTERISTICS OF GLOBULAR PROTEIN.

A

GLOBULAR PROTEIN:
- IT FORM A FUNCTIONAL COMPONENT IN THE BODY
- INSOLUBLE IN WATER
- COMPACTLY FOLDED AND COILED
- EXAMPLE: ALBUMIN, GLOBULIN, INSULIN, ENZYME

22
Q

STATE THE CHAACTERISTICS OF FIBROUS PROTEIN.

A

FIBROUS PROTEIN:
- IT FORM THE STRUCTURAL COMPONENT IN THE BODY
- IT HAS A LONG, ROD SHAPED
- IT IS SPIRAL AND HELICAL AND ARE CROSS LINKED BY THE DISULFIDE BOND AND HYDROGEN BOND
- PHYSICALLY TOUGH
- EXAMPLE: KERATIN, ELASTIN, COLLAGEN, FIBRIN

23
Q

STATE THE CLASSIFICATION OF PROTEIN BASED ON SHAPE.

A
  1. FIBROUS PROTEIN
  2. GLOBULAR PROTEIN
24
Q

STATE THE CLASSIFICATION OF PROTEIN BASED ON ITS COMPOSTION.

A
  1. SIMPLE PROTEIN
  2. COMPLEX PROTEIN
  3. DERIVED PROTEIN
25
Q

WHAT IS SIMPLE PROTEIN?

A

SIMPLE PROTEIN:
- COMPOSED OF ONLY AMINO ACID
- EXAMPLE: ALBUMIN, GLOBULIN, HISTONE

26
Q

STATE THE TYPES OF GLOBULIN

A
  1. ALPHA 1 GLOBULIN - ANTITRYPSIN
  2. ALPHA 2 GLOBULIN - HAPOGLOBULIN
  3. BETA GLOULIN - TRANSFERRIN
  4. GAMMA GLOBULIN - IMMUNOGLOBULINS
27
Q

WHAT IS COMPLEX PROTEIN?

A

COMPLEX PROTEIN:
- IT IS A PROTEIN THT CONSIST OF AA AND ALSO OTHER ORGANIC COMPOUNDS
- THT NON AMINO GRP IS KNOWN AS PROTHETIC GRP.

28
Q

WHAT IS DERIVED PROTEIN?

A

DERIVED PROTEIN:
- IT IS A DENATURED PROTEIN THAT ARE DERIVED FROM THE SIMPLE AND CONJUGATED PROTEIN THAT OCCUR INACTIVE PROTEIN AND ENZYMES ARE BROKEN DOWN INITIALLY TO PEPTIDES BY THE INTRACELLULAR PROTEOLYTIC ENZYMES
- THEY ARE DEGRADED INTO AMINO ACIDS WITHIN THE CELLS FOR RESYNTHESIS OF NEW PROTEINS.

29
Q

STATE EXAMPLES OF PROTEIN FOR EACH OF THESE FUNCTION:
1. MOTILITY
2. STRUCTURAL
3. ENZYMES
4. TRANSPORT PROTEIN

A
  1. MOTILITY: TUBULIN, ACTIN, MYOSIN
  2. STRUCTURAL: ELASTIN, COLLAGEN, KERATIN
  3. ENZYMES: DNA POLYMERASE
  4. TRANSPORT PROTEIN: HAEMOGLOBIN
30
Q

STATE EXAMPLES OF PROTEIN FOR EACH OF THESE FUNCTION:
1. HORMONES
2. CELL SURFACE RECEPTOR
3. NEUROTRANSMITTER
4. IMMUNOGLOBULINS

A
  1. HOMRONES: INSULIN
  2. CELL SURFACE RECEPTOR: INSULIN
  3. NEUROTRANSMITTER: ENDORPHINS
  4. IMMUNOGLOBULINS: ANTIBODIES

BIOMOLECULAR (17 decks)

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