MCS Flashcards
(479 cards)
What is conformation?
Unique 3D shape of a protein
- Conformation depends on amino acid sequence
FUNCTIONS: (7)
1) Enzymatic catalyst
2) Systematic movement ( muscles)
3) Transport and storage of small molecules and ions.
4) Mechanical System ( skin and bones)
5) Immune system ( Anti bodies)
6) Communication:
- Hormones: Some hormones are proteins
-cellular receptors and neurotransmitters are proteins
7) Growth and Differentiation( Controlling gene expression):
- Repressor proteins supress DNA sequences
- Transcription and Translation.
All amino acids are optically active, except which one?
Glycine
What is an Imino acid?
An amino acid with a secondary amino group..
What is an example of an imino acid?
Proline.
What configuration is required for amino acids to be optically active?
L configuration.
What is D- configuration?
Bacteria and Invertebrates.
What does amphoeteric mean?
BOTH acidic and basic properties.
- amphoteric properties, depend on how easily side chains dissociate.
What is a “left handed isomer” classified as?
L isomer
What is a “right handed isomer” classified as?
D isomer.
isoelectric point:
Point at which overall charge of protein is ZERO
Are proteins branched or unbranched
Proteins are unbranched polymers.
What is a “residue” ?
Amino acid in a poly peptide chain.
Poly peptides are formed by what type of reaction?
Condensation.
When is an amino acid protanated/deprotanated?
If ph is higher than pka, then it is deprotonated.
If ph is lower than pka, then it is protonated.
Globular:
tight folding poly peptide chains.
SOLUBLE
Fibrous:
Straight poly peptide chains forming fibres or sheets
INSOLUBLE.
STRUCTURE? Covalent, back bone
and amino acid sequence:
Primary Structure
STRUCTURE? Bonds between other neighbouring residues
Secondary strucure
Bonds involved in the Secondary structure
Hydrogen bonding
Ultimately, forming alpha helix or beta pleated sheets
Hydrogen bonding (HELICAL):
If the h-bonds form between peptide bonds in the SAME CHAIN.
Hydrogen bonding( EXTENDED structures):
If h-bonds form between peptide bonds in different chains.
Alpha helix brief description:
Rod like structures with peptide bonds coiled tightly inside.
- side chains face outwards
- coils turn in a clockwise direction.
- There are 3.6 residues, per turn of helix.
Beta- pleated sheets
c-c bonds are tetrahedral
chains lay side by side
- chains may run in the “same directions” ( Parallel beta sheets)