If ID is false, why can we detect human engineered virii?

There is a strong suspicion the coronavirus is an escaped specimen from a Chinese lab.

https://www.biorxiv.org/content/10.1101/2020.01.30.927871v1.full.pdf

An Indian scientist has purportedly discovered HIV inserted into the coronavirus. If true, this is pretty conclusive evidence the virus is humanly engineered, i.e. intelligently designed.

So, herein lies the conundrum. According to popular imagination, ID is both bad science and false (remember, good science is the falsifiable sort ;). If true, then it should not be possible to detect intelligent intervention in the genetic code.

Yet, this recent news item purports to be exactly that: identification of intelligent intervention in the genetic code.

Please explain this to me like I am 5: how can ID be both bad science and false, yet at the same time it is possible to identify intelligent intervention in the genetic code? If we can do so for the recent past, why can’t we do the same for the distant past?

Thanks!

0

162 thoughts on “If ID is false, why can we detect human engineered virii?

  1. colewd: Are you claiming this as a general rule :-). I think you need to cite papers of eukaryotic cells more often.

    No, I don’t need to do that because the introduction to that paper is general to what is known about proteins and not exclusive to prokaryotes at all. You’d know that if you bothered to read it instead of just the title.

    The amino acid glycine doesn’t magically alter it’s properties just because it’s inside a eukaryotic cell instead of a prokaryote. None of them do. The fundamental forces like electromagnetism, the physical basis for chemical bonds, is not altered in different organisms. Electrons are still attracted by protons, DNA still forms a double helix, and bases still perform Watson-Crick base-pairing.

    0
  2. colewd: Why in the world would someone with your intelligence and education make such claims? Where is the win here?

    We know why someone with your intelligence and your education can’t grasp the simplest concepts in evolutionary biology despite having them explained to you a hundred times.

    0
  3. Rumraket,

    The amino acid glycine doesn’t magically alter it’s properties just because it’s inside a eukaryotic cell instead of a prokaryote. None of them do. The fundamental forces like electromagnetism, the physical basis for chemical bonds, is not altered in different organisms. Electrons are still attracted by protons, DNA still forms a double helix, and bases still perform Watson-Crick base-pairing.

    We have many examples of multiple binding in proteins in eukaryotic cells including cell replication and regulation. We also know where changes cause cells too fail. Your claim is not broadly supported and is probably also not supported for prokaryotic cells.

    0
  4. colewd: We have many examples of multiple binding in proteins in eukaryotic cells including cell replication and regulation. We also know where changes cause cells too fail. Your claim is not broadly supported and is probably also not supported for prokaryotic cells.

    Bill repeats more sciency words he heard which he has no idea the meaning of. But Bill “answered” so he did his Jesus Duty for today. 🙂

    0
  5. colewd: So a 2 digit lock is as hard to beak as a 10 digit lock.

    Yes! That’s right!
    So long as the 10 digit lock has 100 billion combinations that will open it; this is what we mean by ‘sparseness’.

    A protein binding ATP is as easy as a protein that interacts with 10 different proteins?

    As Rumraket noted, protein-protein interactions are very easy to start, a lot easier than binding a small molecule ligand with high specificity. With protein-protein interactions, the tough thing is getting the little bastards to stop. That’s why biochemists faff around adding BSA or surfactants to their precious purified proteins — otherwise they’ll aggregate. Read Carija et al 2019.

    Why in the world would someone with your intelligence and education make such claims? Where is the win here?

    Err, thank you, I guess. The hope is that, eventually, you will realize that we do know what we are talking about and that gpuccio et al do not.

    1+
  6. colewd: We have many examples of multiple binding in proteins in eukaryotic cells including cell replication and regulation. We also know where changes cause cells too fail. Your claim is not broadly supported and is probably also not supported for prokaryotic cells.

    Wrong. Read the paper. It’s all there in the introduction which makes numerous references to the literature that shows protein aggregation is a general phenomenon in both prokaryotes and eukaryotes.

    0
  7. Rumraket,

    Wrong. Read the paper. It’s all there in the introduction which makes numerous references to the literature that shows protein aggregation is a general phenomenon in both prokaryotes and eukaryotes.

    My claim has nothing to do with protein aggregation. You and Jock are both going off on tangents to avoid facing the real facts. This could be the beginning of Texas sharper shooter 2 and I don’t think that’s a good use of our time.

    0
  8. DNA_Jock,

    Err, thank you, I guess. The hope is that, eventually, you will realize that we do know what we are talking about and that gpuccio et al do not.

    You and Rum are smart articulate guys and so is gpuccio. This is like watching the dems and republicans battle.

    0
  9. colewd: My claim has nothing to do with protein aggregation.

    What you mean to say is that you think that your claim has no relation to protein aggregation, and we are telling you that you are wrong.

    And that you should read the paper I referenced because the introduction gives a nice short overview of the state of knowledge of the field of protein aggregation(other papers are referenced there where the phenomenon has been studied both in vitro and in eukaryotic cells), and if you want more in-depth explanations for the biophysical basis of protein-protein interactions(which aggregations are), you’re going to have to read the references given there in the introduction, and to extend and develop what you learn there probably also a good textbook on molecular biology.

    We are really not telling you this to be “articulate and smart” elitist arseholes, but because it is true. It’s good science, it has very strong empirical support. There are good reasons in the physics and chemistry of chemical bonds for why this is so.

    0
  10. Rumraket,

    And that you should read the paper I referenced because the introduction gives a nice short overview of the state of knowledge of the field of protein aggregation(other papers are referenced there where the phenomenon has been studied both in vitro and in eukaryotic cells), and if you want more in-depth explanations for the biophysical basis of protein-protein interactions(which aggregations are), you’re going to have to read the references given there in the introduction, and to extend and develop what you learn there probably also a good textbook on molecular biology.

    Proteins can aggregate in cells I got it. This is observed in neurodegenerative diseases like Parkinson’s. This has nothing to do with proteins operating with multiple binding partners to form a function such as cell division. My point that proteins that have multiple functional binding partners are more functionally restrictive than proteins that bind single molecules. The conservation data supports this hypothesis so far. I was not clear with the claim up front and this caused the discussion to side track. Sorry.

    0
  11. colewd to DNA_Jock,
    You and Rum are smart articulate guys and so is gpuccio.

    Sure. I could appreciate that gpuccio was a smart and articulate guy. I could also notice that he overestimated his smarts and thought he understood things much better than he really did. I still thought we was well-intentioned in his mistaken notions, and I thought it would be possible to have a real conversation with the guy. I have thus learned that honesty doesn’t come together with smarts and articulation. It’s not possible to have a real conversation with the guy. His dishonesty gets in the way.

    By the way:

    colewd to Rumraket,
    We have many examples of multiple binding in proteins in eukaryotic cells including cell replication and regulation.We also know where changes cause cells too fail. Your claim is not broadly supported and is probably also not supported for prokaryotic cells.

    This has nothing to do with what Rum said. However, I’d like to point out that gpuccio said, adamantly, that affinity has nothing to do with how proteins work (he might imagine that proteins work together and recognize their substrates by telepathy). Therefore, you’re contradicting the guy. If proteins bind to each other, then they have affinity to each other, and then affinity has a lot to do with it. Which is it?

    0
  12. colewd: This is observed in neurodegenerative diseases like Parkinson’s. This has nothing to do with proteins operating with multiple binding partners to form a function such as cell division.

    And this is exactly where you are wrong, because the underlying principle is the same. Binding between proteins is a function of the mutual affinity of the shape and distribution of charge on their surface.

    It is the very same thing that makes proteins aggregate, as it is that makes proteins bind each other in some particular beneficial function.

    It turns out that in actual fact, most proteins have some native low level of affinity to each other, particularly in the crowded interior of a cell(important link, read it. Here’s a review article on that same subject.) where most proteins are more or less forced up against each other most of the time.
    So at any given moment, most proteins in the cell are undergoing some level of interaction with all the other proteins pushing up against them in their surroundings. Should any of these interactions turn out to be useful, they can be further enhanced by natural selection.

    So it actually turns out that among a large ensemble of constant protein-protein interactions, selection merely has to enhance those that are beneficial. It doesn’t really have to “find” the interactions first by some blind mutational search from a state of no no intitial association and then sort of add them up one at a time. Instead, a protein has dusins and dusins of potential, native, though often transient interactions, from which the useful ones will be amenable to enhancement by natural selection.

    You would know and understand this if you actually bothered to read the paper, the references given there, and perhaps more importantly, a textbook on biochemistry that has a chapter on protein-protein interactions and association constants.

    1+

Leave a Reply

This site uses Akismet to reduce spam. Learn how your comment data is processed.