Protein Metabolism, Turnover and Synthesis Flashcards

(27 cards)

1
Q

what % of total body protein is turned over daily?

A

1-3%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what are the four main functions of proteins?

A

form new muscle cells.
form synthetic pathways.
form plasma proteins, immune cells and haemoglobin.
form new enzymes in the gut and digestive system.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what two processes does protein turnover involve?

A

protein synthesis and protein degradation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

what is nitrogen balance?

A

we lose approx 35-100g of protein per day, we need to balance this.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what is a negative nitrogen imbalance?

A

when there is more breakdown than synthesis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what is a positive nitrogen imbalance?

A

when there is more synthesis than breakdown.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

what does half life mean?

A

refers to how long it takes before half of the total amount of protein is broken down, differs in different tissues.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

what are proteins made up of?

A

amino acids (AAs) linked together by peptide bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

what is a peptide?

A

a chain of AAs, usually only about 3 AAs long any longer is a protein.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what are peptide bonds?

A

covalent bonds formed through a dehydration synthesis (condensation) reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

what is the primary structure of a protein?

A

simply the order of the amino acids.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

what is the secondary structure of a protein?

A

the amino acid chain wraps around itself forming the helix structure proteins are famous for.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what is the tertiary structure of a protein?

A

the chain of peptides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what is the quaternary structure of a protein?

A

assembly of the tertiary subunits.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

how do proteins have different functions?

A

the order of the amino acids allows different proteins to have different functions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

how many functions do proteins have?

A

there is no protein in the universe which has multiple, every single protein only has one unique function.

16
Q

why is it useful for the half life to differ in different tissues?

A

some cells such as those in the liver have a very quick half life, this is useful because the liver is in charge of getting rid of toxic substances therefore getting them gone as quickly as possible whereas others such as mitochondrial and myofibrillar proteins take a long time, this is useful because we could lose all of our muscle overnight if these broke down too quickly therefore it maintains our muscles.

17
Q

what is hypertrophy and what causes it?

A

increase in muscle size - going to the gym repetitively. this results from the accretion of new proteins in the muscle fibre.

18
Q

how does cardio-respiratory training help us to become stronger and fitter?

A

cardio-respiratory and resistance training can up regulate proteins in skeletal muscles, for growth to take place the muscle protein synthesis must exceed breakdown.

19
Q

what are genes?

A

sections of our DNA that code for a specific protein, contain the information required to make new proteins.

20
Q

explain transcription

A

transcription takes place when a signal from outside the cell (transcription factor) initiates the duplication of a section of DNA, the double-stranded helix is separated and transcribed by RNA Polymerase II creating the single stranded mRNA. this is replicated via the base pairs matching, A with U, T with A, C with G, and G with C. (adenosine, thymine, uracil, cytosine, guanine - thymine does not occur on RNA therefore A pairs with uracil in transcription)

21
Q

explain translation

A

mRNA leaves the nucleus and goes to a ribosome where each codon (three bases) codes for a specific amino acid. the tRNA molecule comes along with matching anticodons and the corresponding amino acids. once the anticodons bond with the codons the amino acid is released forming a chain which will later be folded and create a new protein. this continues until the ‘stop’ codon which means the end of the protein.

22
Q

how does repeated training cause muscle growth?

A

when exercise is repeated over time new proteins are formed causing hypertrophy. however, it is not the actual exercise which causes this muscle growth but rather the fact that when we exercise we are actually breaking down muscle, it is therefore the rebuilding process which makes the muscles bigger.

23
Q

what are the two main pathways for protein degradation?

A

the lysosomal pathway and the ubiquitin pathway.

24
what are the pathways for protein degradation used for, give an example?
to rid the body of damaged or abnormal proteins, essentially replacing them with newer and better versions. e.g. in exercise muscle damage where intracellular proteins such as dystrophin, are damaged and therefore degraded after exercise so new ones can be built (protein synthesis).
25
what is a ubiquitin protein?
an abnormal / damaged protein. proteins can be tagged for degradation by the addition of a chemical marker called ubiquitin. ubiquitin-tagged proteins are taken to the proteasome, or "recycling centre" of the cell, and broken down into their component parts.
26
what are lysosome proteins?
extracellular proteins, cellular organs and membranes. protease enzymes degrade the proteins in the lysosome.