STRUCTURE AND F(X) OF AMINO ACIDS, PEPTIDES, AND PROTEINS Flashcards
___ AND ___ ARE THE FUNCTIONAL GRP OF AMINO ACIDS.
- AMINO GRP
- CARBOXYL GRP
R GRP WILL DETERMINE THE ___ AND ___ OF AN AMINO ACID
- STRUCTURE
- PROPERTIES
STATE THE PROPERTIES OF AMINO ACIDS.
- STEREOISOMERS
- AMPHOTERIC
- HAS ITS OWN PK VALUE
- EXIST AS ZWITTERION
- HAS ITS OWN ISOELECTRIC POINT
WHAT IS MEANT BY AMPHOTERIC?
- IT CAN EXIST AS BOTH ACID AND BASE
PROTEIN USUALLY ARE (D/L) ISOMERS
L ISOMERS
STATE THE CHARACTERISTICS OF NON POLAR SIDE CHAIN.
- IT IS DIVIDED INTO 2 WHICH ARE:
- ALIPATHIC (GLYCINE, ALANINE, VALINE, LEUCINE, ISOLEUCINE)
- AROMATIC (PHENYLALANINE, TYROSINE, TRYTOPHAN) - IT DOES NOT FORM A HYDROGEN BOND
- IT PROMOTES THE HYDROPHOBIC INTERACTION - STABALISING THE PROTEIN STRUCTURE
- IT DOES NOT BIND OR DONATE PROTON/ PARTICIPATE IN HYDROGEN OR IONIC BOND.
- LOCATION: ON SURFACE OF MEMBRANE PROTEIN, INTERACT WITH THE LIPIDS
STATE THE CHARACTERISTICS OF POLAR UNCHARGED SIDE CHAIN.
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
STATE THE CHARACTERISTIC OF ACIDIC SIDE CHAIN.
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
STATE THE CHARACTERISTICS OF BASIC SIDE CHAIN.
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
STATE THE AMINO ACID THAT HAVE NON POLAR SIDE CHAIN.
AROMATIC GRP:
1. PHENYLALANINE
2. TYROSINE
3. TRYTOPHAN
ALIPATHIC GRP:
1. GLYCINE
2. ALANINE
3. VALINE
4. LEUCINE
5. ISOLEUCINE
STATE THE AMINO ACID THAT HAVE POLAR UNCHARGED SIDE CHAIN.
- THREONINE
- CYSTEINE
- SERINE
STATE THE AMINO ACID THAT HAVE ACIDIC SIDE CHAIN.
- GLUTAMATE
- ASPARTATE
STATE THE AMINO ACID THAT HAVE BASIC SIDE CHAIN.
- LYSINE
- ARGININE
- HISTIDINE
STATE THE CLASSIFICATION OF AMINO ACID BASED ON ITS SIDE CHAIN
- POLAR UNCHARGED SIDE CHAIN
- NON POLAR SIDE CHAIN
- ACIDIC SIDE CHAIN
- BASIC SIDE CHAIN
STATE THE CHARACTERISTICS OF PRIMARY STRUCTURE OF PROTEINS.
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.
STATE THE CHARACTERISTICS OF SECONDARY STRUCTURE OF PROTEIN.
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.
STATE THE CHARACTERISTICS OF TERTIARY STRUCTURE OF PROTEIN.
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
DESC THE TERTIARY STRUCTURE IN MYOGLOBIN.
- 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.
DESC THE CHARACTERISTICS OF QUATERNARY STRUCTURE.
- 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
COMPARE HAEMOGLOBIN AND MYOGLOBIN.
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.
STATE THE CHARACTERISTICS OF GLOBULAR PROTEIN.
GLOBULAR PROTEIN:
- IT FORM A FUNCTIONAL COMPONENT IN THE BODY
- INSOLUBLE IN WATER
- COMPACTLY FOLDED AND COILED
- EXAMPLE: ALBUMIN, GLOBULIN, INSULIN, ENZYME
STATE THE CHAACTERISTICS OF FIBROUS PROTEIN.
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
STATE THE CLASSIFICATION OF PROTEIN BASED ON SHAPE.
- FIBROUS PROTEIN
- GLOBULAR PROTEIN
STATE THE CLASSIFICATION OF PROTEIN BASED ON ITS COMPOSTION.
- SIMPLE PROTEIN
- COMPLEX PROTEIN
- DERIVED PROTEIN
WHAT IS SIMPLE PROTEIN?
SIMPLE PROTEIN:
- COMPOSED OF ONLY AMINO ACID
- EXAMPLE: ALBUMIN, GLOBULIN, HISTONE
STATE THE TYPES OF GLOBULIN
- ALPHA 1 GLOBULIN - ANTITRYPSIN
- ALPHA 2 GLOBULIN - HAPOGLOBULIN
- BETA GLOULIN - TRANSFERRIN
- GAMMA GLOBULIN - IMMUNOGLOBULINS
WHAT IS COMPLEX PROTEIN?
COMPLEX PROTEIN:
- IT IS A PROTEIN THT CONSIST OF AA AND ALSO OTHER ORGANIC COMPOUNDS
- THT NON AMINO GRP IS KNOWN AS PROTHETIC GRP.
WHAT IS DERIVED PROTEIN?
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.
STATE EXAMPLES OF PROTEIN FOR EACH OF THESE FUNCTION:
1. MOTILITY
2. STRUCTURAL
3. ENZYMES
4. TRANSPORT PROTEIN
- MOTILITY: TUBULIN, ACTIN, MYOSIN
- STRUCTURAL: ELASTIN, COLLAGEN, KERATIN
- ENZYMES: DNA POLYMERASE
- TRANSPORT PROTEIN: HAEMOGLOBIN
STATE EXAMPLES OF PROTEIN FOR EACH OF THESE FUNCTION:
1. HORMONES
2. CELL SURFACE RECEPTOR
3. NEUROTRANSMITTER
4. IMMUNOGLOBULINS
- HOMRONES: INSULIN
- CELL SURFACE RECEPTOR: INSULIN
- NEUROTRANSMITTER: ENDORPHINS
- IMMUNOGLOBULINS: ANTIBODIES
