Protein Flashcards

0
Q

what is the arrangement like in alpha helices?

A

side chains always facing outwards
N-H bonds always face upwards and the C=O bonds always face downwards
looks like a coil with a very repetitive arrangement of amino acids- 3.6 amino acids for every coil

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1
Q

what is the secondary structure of proteins?

A

different folding by hydrogen bonds

beta pleated sheets and alpha helices

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2
Q

what do beta-pleated sheets look like ?

A

rows of amino acids on top of one another, running in anti-parallel directions

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3
Q

what does the tertiary structure of proteins involve?

A

3D folding of the secondary structure

bonds involved are ionic bonds, hydrogen bonds, van der waals forces and also sulphur bridges

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4
Q

which strand of DNA is mRNA a copy of ?

A

coding strand

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5
Q

which direction is the RNA strand elongated in during transcription?

A

5’ to 3’ direction

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6
Q

why is it not a problem that transcription is a lot less accurate than DNA replication?

A

because a lot more RNA can be produced and also the DNA has to store genetic info indefinitely

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7
Q

what are the different types of RNA polymerase ?

A

type 1,2 and 3
1 + 3 are used to transcribe genes encoding rRNA and tRNA
2 is used to transcribe all other proteins

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8
Q

what is needed to allow RNA polymerase to transcribe a gene ?

A

transcriptional activators to activate RNA polymerase
requires mediators to communicate between different proteins
chromatin modifying enzymes to allow DNA to be reached from inside chromatin

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9
Q

what is the process called that splices exons together ?

A

transesterification

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10
Q

how many different combinations of codons are there for an RNA strand?

A

64 because there are 4 different nucleotides and they are read in threes

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11
Q

what does it mean by the genetic code being redundant ?

A

there are 64 combinations of codons but only 20 different amino acids therefore different codons can code for the same amino acid

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12
Q

what enzyme attaches the correct amino acid to the tRNA molecule?

A

aminoacyl-tRNA synthetase

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13
Q

what is fetal haeomoglobin made up of and what effect does this have ?

A

made up of 2 alpha-2 subunits and 2 gamma-2 subunits
makes it have a higher affinity for oxygen compared to maternal adult haemmoglobin so it is able to extract oxygen from the maternal circulation

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14
Q

what chromosomes are the embryonic Hb gene, alpha gene, delta gene, beta gene and gamma fetal gene present on ?

A

embryonic and alpha gene- chromosome 16

delta, beta and fetal gamma gene- chromosome 11

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15
Q

which type of glycosylation is most common?

A

N-glycosylation -90%

16
Q

what effects can phosphorylation have on a protein ?

A

addition of a phosphate molecules causes the addition of 2 negative charges which causes conformational changes in the protein
negative charges can attract positively charged molecules which can affect ligand binding of the protein

17
Q

what is myristoylation?

A

attachment of a myristate molecule to a glycine amino acid
myristate is a 14 carbon fatty acid molecule
occurs in cytosol
important in interactions of proteins with the membrane and other proteins

18
Q

what is ubinquitation ?

A

addition of a ubiquitin molecule to a protein

normally attaches to lyseine

19
Q

what is sickle cell anaemia ?

A

autosomal recessive disorder

develops when fetal Hb is being converted into adult Hb due to a mutation in the beta subunit

20
Q

what does sickle cells anemia cause ?

A

it causes deoxygenated Hb to produce insoluble filaments within RBCs causing their disfiguration so they cant pass through capillairies very easily
if they get blocked they can cause oxygen depletion at tissues