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Elena L [17]
2 years ago
12

What could happen if a mutation in a gene caused a hydrophobic amino acid in a polypeptide to be replaced by a hydrophilic amino

acid?
Biology
1 answer:
Marysya12 [62]2 years ago
3 0

The new hydrophilic amino acid would not form the same interactions with hydrophobic R groups. As a consequence,   protein's 3D structure would likely be affected.

Different types of amino acids have different properties and thus form different interactions. For example, hydrophobic amino acids (water-repelent) such as alanine, valine, leucine, isoleucine, proline, phenylalanine, cysteine and methionine. participate in van der Waals type of interactions. They often form the hydrophobic core of the protein which doesn’t interact with water surrounding.

On the other hand, hydrophilic amino acids (arginine, asparagine, glutamine, aspartat..) are polar, can dissolve in the water and can join the hydrogen bond network.

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Answer:

C

Explanation:

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So base on the question that states and ask to give the name of one cell type that continues to divide throughout a person's lifetime and also on who does not, with that question, the cell that divide through persons lifetime is a Mitosis or skin cells, an example to this is the skin, and the who doesn't divide is i think the brain cells, it doesn't regenerate
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3 years ago
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seropon [69]

Answer:

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Explanation:

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How to get high affinity antibody?
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Human monoclonal antibody (mAbs) are emerging in the field of cancer therapy and have become an increasing proportion of new drugs that are recently approved. Although there are some methods to obtain antigen-specific mAbs from human B cells, it is generally impossible to directly immunize human beings with antigens of interest. For example, for infectious agents, those approaches are largely restricted. To solve these obstacles, two main approaches have been developed; either by humanizing antigen-specific antibodies from small experimental animals (which is laborious due to the great genetic differences from humans) or rely on the in vitro selection of antigen-specific binders from human antibody repertoires. However, the human mAbs developed by these methods are usually with low affinity.

We are now coming up with a much better idea that is humanizing non-human primates mAbs instead of murine mAbs. Due to the close genetic relationship with humans, immunized NHPs have more potential to be isolated with high affinity antibody to human target than other experimental species, such as mouse, rat and rabbit. In addition, with appropriate method, NHP antibodies are much<span> easier to be humanized</span> without any loss of affinity compared to widely used murine antibodies. 

Resource: http://www.creative-biolabs.com/High-Affi-TM-Human-Antibody-Discovery.html

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