Of the answers below, what is the smallest nucleotide sequence that could code for a protein with 300 amino acids?

1 answer:

6 0

The nucleotide sequence would have to have 900 nucleotides in order to code for a protein of 300 amino acids. When translating RNA into proteins, RNA is read 3 bases at a time. Each group of 3 bases is a codon, and each codon codes for an amino acid. When read, the proper amino acid is added to a growing chain of amino acids, which will be folded to become a protein.

Therefore, 300 amino acids * 3 nucleotides per amino acid = 900 nucleotides.

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A protein has a molecular mass of 400 kDa when measured by gel filtration. When subjected to gel electrophoresis in the presence

RoseWind [281]

Answer:

subunit composition

how many: 4 subunits
what sizes: 160 kDa, 60 kDa, 90 kDa, and 90 kDa.

Explanation:

SDS is a detergent that denaturalizes the protein and sets a relation charge size, such as that the motion of the protein in the gel is proportional to its weight. However, the detergent can not disrupt disulfide bridges, so these bonds remain together. The bigger the protein is, the stronger interaction with the polyacrylamide gel there will be. The speed of displacement in the electromagnetic field is inversely proportional to the protein size.

On the other hand, b-mercaptoethanol acts as a reductive agent, breaking disulfide bonds. This chemical produces a complete denaturalization resulting in the unfolded protein. If disulfide bridges kept two protein subunits together, the b-mercaptoethanol separates them.

So, the most important data we need to consider here is that SDS can not disrupt disulfide bridges, while b-mercaptoethanol can.

Available data:

A protein has a molecular mass of 400 kDa
SDS → three bands with molecular masses of 180, 160, and 60 kDa
SDS + b-mercaptoethanol → three bands with molecular masses of 160, 90, and 60 kDa

SDS

180 + 160 + 60 = 400 kDa

SDS + b-mercaptoethanol

160 + 90 + 60 = 310 kDa

The difference between them is 400 - 310 = 90 kDa, meaning that there is a subunit of 90 kDa that is not being detected by SDS alone.

From both measures ( SDS and SDS/b-mercaptoethanol) we can assume that subunits 160 kDa and 90kDa are the same. So the difference is in the left subunit ⇒ 180 and 90, respectively.

180 - 90 = 90 kDa

We can assume that the 180 kDa subunit is composed of two 90 kDa subunits joined by a disulfide bridge. SDS alone could not disrupt this bond, so it detected a unit of 180kDa. b-mercaptoethanol detected this bond and broke it, generating two 90 kDa units, which migrated together in the gel, so they were expressed as the same band.

This difference suggests that the protein is formed of 4 subunits. One of them is 160 kDa, another one is 90 kDa, and the last two subunits are 90 kDa each.

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True or false, the more elliptical the stain, the more accurate the definition of directionality

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The answer is true, if something in coming at you from a steep direction, there will me more of a long oval shape rather than it hitting you head on making a circle

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4 years ago

A student designs an experiment to test substances X, Y, and Z, to determine which one is a catalyst for the reaction: A + B ® C

VLD [36.1K]

Thank you for posting your question here. Below are the choices:

The test tube that stops bubbling first contains the catalyst.
The test tube that produces the most bubbles contains the catalyst.
The test tube that bubbles the longest contains the catalyst.
The test tube that does not bubble contains the catalyst.

The answer is "The test tube that stops bubbling first contains the catalyst."

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Natural gas I an sure the answer is that

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