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Eco ri methylase
Not a restriction endonuclease
isoelectric point
the specific pH where a molecule (protein/ amino acid) has no net electrical charge
pH value below isoelectric point
proteins arent negatively charged
Michaelis menten model
DOESNT assume the formation of a covalent intermediate between enzyme and substrate
standard alpha helix
3.6 amino acid residues per turn
bacteria transformed with the vector pBR322
grow in the presence of ampicillin
bond that joins nucleotides in RNA
phosphodiester bonds
suitable units for specific activity
micro mole of product/min/mg protein
when are membrane proteins usually inactive
in gel phase lipid
how does N-linked glycosylation occur
primarily via the amide nitrogen atom of asparagine residues
where is peptidoglycan present
cell walls of both gram positive(much thicker) and gram negative bacteria
Beta-mercaptoethanol function
reduce disulphide bridges
T4-DNA ligase requires what for its action
ATP
what can membrane proteins contain
beta barrels
how does lactose get digested in the absemce of glucose
lactose converted to allolactose- bind to lac repressor, changing shape and preventing access to operons genes- turns them on to digest lactose
what reduces disulphide bridges
Beta-mercaptoethanol
Type 2 restriction enzymes
cleave at their specific recognition sites in DNA
ninhydrin
turrns yellow when amide groups present
where does amino acyl-tRNA bind in ribosome
A- site
peptide bond property
planar
cellulose
polymer of glucose monomers joined by beta- linkages
how many residues does a transmembrane alpha helix contain
20
Michaelis menten model assumes what?
E«S
direction of protein synthesis
from amino (N) terminus to the carboxyl (C ) terminus
Electrophoresis in absence of SDS
separates molecules according to their charge and mass
Trypsin
cleaves proteins on the carboxyl side of lysine or arginine residues
Alpha helices are destabilised by what?
glycine residues
RNA polymerase initiates synthesis of mRNA how?
bind to promoter region
how are alpha helices staabilised
by hydrogen bonds between residue x and residue x+ 4
Expression vectors
used to make eukaryotic proteins in prokaryotic hosts
Maximum rate of reaction (Vmax )
the point where all the active sites are bound to substrate (enzyme is saturated)
reflects how fast the enzyme can catalyse the reaction
if a low value- enzyme does not convert much substrate to product per unit time when enzyme saturated with product
Michaelis constant (Km)
the substrate concentration which is equal to half its maximum value
a low value means only a small amount of substrate is required to saturate the enzyme indicating high affinity for the substrate