Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
52 Cards in this Set
- Front
- Back
T/F - Proteins are greater than 50 amino acid chains long
|
True
|
|
T/F Polypeptides are classified as either being less than 50 amino acids long or Being ACTIVE
|
False - they are either <50 AA long or INACTIVE (or both)
|
|
What are the structural elements that amino acids always contain?
|
Central C Carbon
Amine group attached to a-carbon of a carboxylic acid R Group Side chain Carboxylic acid |
|
How many amino acids are central to the Genetic code?
|
20
|
|
Which derivation L-amino acids or D-amino acids are available in the body but not used?
|
D-amino acids
|
|
What are the 5/20 core amino acids with aliphatic side chains?
|
(GAVLI)
GIVE ALIPHATIC VEINS LIFTING IMPACT Glycine, Alanine, Valine, Leucine, Isoleucine |
|
What is the feature of an aliphatic side chain?
|
Carbon containing side chain - hydrophobic by nature - NON Polar
|
|
What are the 3/20 core amino acids with hydroxylic side chains?
|
(STT)
Serine, Threonine, Tyrosine |
|
What is the feature of Hydroxlic side chains?
|
They contain a hydroxyl group - OH
|
|
What are the 2/20 core amino acids with sulphur side chains?
|
(CM)
Cysteine, methionine |
|
Which 4/20 amino acids contain amino acid groups or their amides as side chains?
|
Aspartic Acid, Asparagine, Glutamic Acid, Glutamine
|
|
What is the distinctive feature of an acidic side group or an amine group?
|
-COOH, -COO-
|
|
What are the 3/20 amino acids with amine (Basic) Side groups?
|
(ALH)
Arginine, Lysine, Histidine |
|
What is the distinctive feature of an amine side group?
|
-NH group
|
|
Which 2 amino acids feature attributes from more than one side chain classifcation?
|
Tyrosine - aromatic + Hydroxylic
Histidine - aromatic + Basic |
|
What are the 4/20 amino acids with aromatic Side groups?
|
(HPTT) - Histidine, Phenylanine, Tyrosine, Trytophan
|
|
What is the unique amino acid structure and which amino acid falls into this category?
|
Imino acid - proline
|
|
What attribute of an amino acid defines its function?
|
It's polarity
|
|
What are the 7 functions of amino acids?
|
Structure, Enzymes, Movement, Transport, Hormones, protection, Storage, Regulation
|
|
How does the structural function manifest in the body?
|
Keratin in Hair and Nails
|
|
How does the enzymatic function manifest in the body?
|
Most bodily reactions are catalysed by enzymes
|
|
How does the movement function manifest in the body?
|
Myosin and actin are what makes our muscles move
|
|
How does the transport function manifest in the body?
|
Haemoglobin transports oxygen from lungs to cells
|
|
How does the Hormone function manifest in the body?
|
Most hormones are proteins - insulin - HGH
|
|
How does the protection function manifest in the body?
|
antibodies fight disease
|
|
How does the storage function manifest in the body?
|
Casein in milk stores nutrients, ferritin in liver stores iron
|
|
How does the regulation function manifest in the body?
|
regulates the expression of genes
|
|
How are proteins classified by composition?
|
Albumoids, albumins, globulins, histones, glycoproteins, lipoproteins, metalloproteins, nucleoproteins, phosphoproteins
|
|
What are examples of albumoid proteins?
|
keratin, collagen - structural proteins
|
|
What are examples of albumins proteins?
|
egg albumin, serum albumin - globular proteins
|
|
What are examples of globulins proteins?
|
antibodies - globular proteins
|
|
What are examples of histones proteins?
|
chromatin in chromosomes - globular proteins
|
|
What are examples of glycoproteins?
|
attached carbohydrates - interferon - globular proteins
|
|
What are examples of lipoproteins?
|
attached triglycerides, phosholipids, cholesterol - globular proteins
|
|
What are examples of nucleoproteins?
|
attached nucleic acids - ribosomes - globular proteins
|
|
What are examples of phosphoproteins?
|
attached phosphate group - casein - globular proteins
|
|
What are examples of metalloproteins?
|
attached metal ion - haemoglobin - globular proteins
|
|
What 2 functional groups do all amino acids contain?
|
Amine group
Carboxylic acid group |
|
How are two amino acid groups attached together?
|
The amine of one AA is joined to the carboxylic acid of the other by amidation (condensation process)
|
|
What is the name and structure of the simplest amino acid?
|
Glycine, Central C - attached to an amine and carboxylic acid group and 2 Hydrogens (R=H)
|
|
What are the four levels of structure of proteins?
|
Primary - sequence of amino acids, Secondary - association of amino acids close by, using Hydrogen Bonding, Tertiary - 3D folded structure, Quaternary - association of monomers with each other
|
|
What are the abbreviations of the A&C Amino acids?
|
Ala (A), Arg (R), Asn (N), Asp (D) , Cys (C)
ARNDC Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine |
|
What are the abbreviations of the GHI Amino acids?
|
Gly (G), Gln (Q), Glu (E), His (H), Ile (I),
GQEHL, Glycine, Glutamine, Glutamic Acid, Histidine, Isoleucine |
|
What are the abbreviations of the LMP Amino acids?
|
Leu (L), Lys (K), Met (M), Phe (F), Pro (P),
LKMFP, Leucine, Lysine, Methionine, Phenylalanine, Proline |
|
What are the abbreviations of the STV Amino acids?
|
Ser (S), Thr (T), Trp (W), Tyr (Y), Val (V),
STWYV, Serine, Threonine, Tryptophan, Tryrosine, Valine |
|
How is Tyr-Gly-Gly-Phe-Met different from Met-Phe-Gly-Gly-Tyr?
|
The sequencing always go from the start of the molecule, so as the start AA is different they will act differently
|
|
When Glutamic acid is replaced by Val in the haemoglobin structure what happens?
|
The difference in polarity of this AA replacement forces the molecule to fold in a different way.
This impacts the way the body handles this molecule and causes issues - clotting, anaemia and more. |
|
Why is the tertiary structure more important than the primary structure?
|
The monomer's unique shape means that specific proteins are augmented in a specific direction which then interact with enzymes in a specific way. Wrong orientation and the enzymatic reaction will not occur.
|
|
What is denaturation?
|
many things can alter the structure of a protein resulting in a chemical change. ie. Heat, Ph Change, heavy metal ions, solvents, radiation etc,.
|
|
What is the difference between Denaturation and hydrolysis of proteins?
|
Denaturation breaks the bond sin secondary and tertiary proteins, whilst hydrolysis breaks down the protein.
|
|
What are the 9 essential amino acids?
|
VMLLIPTT
Very Merry Lysine Lets Is Phace Through Trips Valine, Methionine, Lysine, Leucine, Isoleucine, Phenylanine, Threonine, Tryptophan |
|
What are the 6 conditionally essential amino acids?
|
Glycine, Histidine, Cysteine, Proline, Arginine, Tyrosine
(Good Histories Can Produce Awful Tempers) |