Mass number = protons + neutrons
If you have the # of protons and the mass #, subtract the number of protons from the mass number to get the number of neutrons.
If you have the number of neutrons and the mass number, subtract the number of neutrons from the mass number to get the number of protons.
Answer:
The correct answer is: d. REs activity is best preserved by freezing the RE and thawing it out for brief periods of time as needed.
Explanation:
- Restriction enzymes can be defined as endonucleases that can recognize specific nucleotide sequence in a DNA (Deoxyribonucleic acid) sequence and cause breakage of phosphodiester bond in the DNA at the target site. Hence, it has the capacity of cleaving a DNA sequence.
- These are made up of proteins which are required to be present in the accurately folded conformation in order to function.
- Any form of alteration in the three-dimensional structure of the protein induced due to physical, chemical, mechanical or physiological factors can cause denaturation of the protein which in turn can render the protein non-functional.
- Freezing of restriction enzymes (REs) directly without the use of glycerol will cause the movement of water molecules within the proteins as well layering of water molecules on the protein surface.
- At low temperature these water molecules change to ice crystals which can alter the conformation of the protein or can cause breakage of peptide bonds in the proteins by physical force.
- This can cause the protein to get denatured and hence non-functional.
- Hence, it is never advisable to preserve REs by freezing directly without glycerol.
- Glycerol forms a layer around the protein molecules and prevents the protein molecules from coming into direct contact with the water molecules and hence prevents protein denaturation.
It takes about one minute for a blood cell to make a complete circuit of the human body.
Answer:
b
Explanation:
Cellular respiration; complementary reaction to photosynthesis, because it's the reaction that cells use to break down glucose molecules and release atp.
The level of the structure is the proteins in the secondary.
<h3>What is the structure of secondary?</h3>
- A polypeptide chain's adjacent amino acid residues are arranged in regular patterns in space, known as secondary structure. It is kept in place by hydrogen bonds between the amide hydrogens and the peptide backbone's carbonyl oxygens. Helixes and structures are the two main secondary structures.
- Local regions of proteins can be organized into one of three three-dimensional configurations: alpha helices (-helix), beta sheets (-strand), or omega loops. The alpha helix is the most prevalent secondary protein shape because it is stable and low-energy.
- The interaction of amino acids with every backbone NH hydrogen bound with the backbone C=O group of the corresponding amino acid residue in the polypeptide chain results in the- helix formation. The- helix motif is particularly prevalent in transmembrane regions of proteins that traverse the lipid bilayer.
You are observing proteins in a lab for an experiment. During transport, they have started to unwind and lose their shape.
The level of the structure is the proteins in the secondary.
To learn more about the secondary structure of a protein, refer to:
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