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Thread: How does the amino acid sequence affect protein folding and bonding? page

  1. #1
    Cindy Hang's Avatar
    Cindy Hang is offline Junior Member
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    How does the amino acid sequence affect protein folding and bonding?

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    Hello friends,

    I want to know how changes in the amino acid sequence of a protein molecule affect its final form. Are there any amino acids which should not be aligned adjacent to one another that sort of thing.

    Best regards
    Cindy Hang

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    sandokan2112's Avatar
    sandokan2112 is offline Member
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    Yes! as a matter of fact there is...

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    otzi's Avatar
    otzi Guest
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    Quote Originally Posted by Cindy Hang View Post
    Hello friends,

    I want to know how changes in the amino acid sequence of a protein molecule affect its final form. Are there any amino acids which should not be aligned adjacent to one another that sort of thing.

    Best regards
    Cindy Hang
    That is probably the best question I have seen here in a long time. Most paleo people lump all amino acids together into a single entity "Protein". By not paying attention to amino acids, which are what make up protein, we leave ourselves open to proteopathy. In my studies, I have found that sequencing is not nearly as important as ensuring that you are consuming the full range of all 9 essential amino acids.

    To form protein, the amino acids are linked by dehydration synthesis to form peptide bonds. The chain of amino acids is also known as a polypeptide. Some proteins contain only one polypeptide chain while others, such as hemoglobin, contain several polypeptide chains all twisted together. The sequence of amino acids in each polypeptide or protein is unique to that protein, so each protein has its own, unique 3-D shape or native conformation. If even one amino acid in the sequence is changed, that can potentially change the protein’s ability to function. For example, sickle cell anemia is caused by a change in only one nucleotide in the DNA sequence that causes just one amino acid in one of the hemoglobin polypeptide molecules to be different. Because of this, the whole red blood cell ends up being deformed and unable to carry oxygen properly. However, since we cannot control the sequencing of amino acids, we are best able to control our cellular biology by providing an environment conducive to protein synthesis, namely folding.

    A proteopathy is a disease that at its core has misfolded proteins in its etiology. The biggest concern is an extreme lack of lipids in the brain. The lipids missing tend to be omega 3 fat variety. But even more interesting it appears the brain needs between 25-35% of omega 3 fats called DHA to function optimally. There also needs to be comorbid neuronal intracellular inflammation present. And we also see up regulation of the IGF-1 pathways and dysregulation of the protein signaling that leads to faulty protein folding in the diseased brain. We used to think the Tau protein that caused the neurofibrillary tangle were the result of the disease but it is becoming clear that the real issue is that these are remnants of faulty protein folding and non functional neurons result. The neurons with these misfolded proteins are toxic and need to be replaced so they undergo apoptosis and the brain’s stem cell supply in the temporal, parietal and frontal lobes become exhausted.

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