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LEVEL 2 BIOCHEM SEM 1 MCQs ANS
LEVEL 2 BIOCHEM SEM 1 MCQs ANS
endoplasmic reticulum/cytoplasm
cytosol
matrix
22. promotes l-leucine oxidation in the skeletal muscle and the
subsequent loss of the oxidized molecules of this amino acid, as
opposed to the reversible transamination reaction that converts
l -leucine into 2-keto-isocaproate.
relevant to tissues
bohr's efect
H.S.R
missense
framesgift
intro of stop
codon
N9-purine
N1-pyrimidine
Not all genes codes for a
protein
not food,maybe fluids
The strand backbones are closer together on one side of
the helix than on the other. The major groove occurs where
the backbones are far apart, the minor groove occurs
where they are close together. The grooves twist around
the molecule on opposite sides. Certain proteins bind to
DNA to alter its structure or to regulate transcription
(copying DNA to RNA) or replication (copying DNA to
DNA). It is easier for these DNA binding proteins to
interact with the bases (the internal parts of the DNA
molecule) on the major groove side because the
backbones are not in the way.
complementary
SUPPOSED TO BE MELATONIN SYNTHESIS
II, VII, IX, and X require posttranslational modification of glutamate
residues to -carboxyglutamate.
FACTOR I
FACTOR VIII
FACTOR IX
FACTOR V
FACTOR III
it caused by defects in the import of peroxisomal matrix
proteins.Mutation in any of the PEX genes has been shown
to block insertion of peroxisomal membrane proteins as well
as import of matrix proteins
It is posttranslational modification
it is synthetic compound
that is structural similar to
adenine
Translation begins at an AUG codon, or sometimes a
GUG.
In Prokaryotes, the modified amino acid N-formyl
methionine is always the first amino acid of the new
polypeptide
Supposed to be
under low oxygen
tension
The end products have been identified as alanine, aspartate,
glutamate, and citrate with -ketoglutarate and oxaloacetate
as intermediate products
...
H.S.R
Co-translational (during translation)e.g. proteins destined to ER,
Golgi, plasma membrane or lysosomes
REGARDS,
H.S.R
PL..