Nobel prize 2024 - magic just got less wriggle room

Because thinking, experiencing and feeling can happen on deeper layers of the mind. It's experience ~ even if you're not directly conscious of it in the moment.

Yes I understand now that "experience" contains these aspects of consciousness as well in the english language but the direct translation of the word experience to danish "erfaring/oplevelse" does not contain these aspects.

Yes I understand now that "experience" contains these aspects of consciousness as well in the english language but the direct translation of the word experience to danish "erfaring/oplevelse" does not contain these aspects.

So it seems, but that does not mean that you cannot use the appropriate set of words to discuss the totality of experience in its manifestations. You just need to think outside of the box.

Different languages can expand your mental horizons with new and unique concepts, so it's useful to understand what different languages can bring to the table, mentally, so to speak.

From https://hinative.com/questions/239771

Oplevelse: an experience. An event of some kind.

Da: Det var en god oplevelse at være i Tivoli i dag.
Eng: It was a good experience to be in Tivoli today.

Erfaring: experience. Knowledge you've gathered personally or in a profession.

Da: Jeg ved ikke om jeg har erfaring nok til mit nye job.
Eng: I don't know if I have enough experience for my new job.

[Laird]

Returning to the first two posts in this thread:

So the protein folding problem turned out to be predictable from purely physical properties after all. No magic realms needed.

I wasn't aware until now that magic realms were being proposed as necessary for protein folding. Can you share more details about this proposal, and who was making it?

In fairness to you, @sbu, I have found somebody who makes the sort of proposal you suggest: Mark Mahin of the Future and Cosmos blog. He has a set of blog posts which deal in protein folding, accessible via the "protein folding" label. I've read the first two that currently show up under that label, the first of which, Misleading Statements in a Recent Nobel Prize Announcement, directly addresses this Nobel Prize.

Based on what I've read in those two posts, Mark contends that the natural shape of proteins is not determined by the genes that code for it. He offers several reasons in support of this contention, including that:

1. Some proteins do not fold into only a single shape, but shift between shapes.
   
2. Some proteins require "chaperones" to fold into their shape.
   
3. Proteins that are "denatured" - meaning that they have lost their natural shape - do not spontaneously fold back into their natural shape.
   
4. The experiments by Christian B. Anfinsen, typically cited as proof for the hypothesis that genes determine final protein shape, were conducted on smaller proteins than average, have anyway failed replication, and are generally of dubious merit.
   
5. The main hypothesis according to which proteins spontaneously fold into their natural shape - i.e., that they strive to minimise the Gibbs free energy of the whole system - fails for a variety of reasons, including that a "search" through the possible energy states would take vast orders of magnitude longer than it actually takes proteins to fold.
   

Regarding the AlphaFold2 programme for which Dennis Hassabis and John M. Jumper won the Nobel Prize, he contends in that first article (linked above), that:

1. AlphaFold2 does not provide any insight into the supposed means by which proteins achieve their three-dimensional structures.
   
2. AlphaFold2, instead, is merely using frequentist prediction: "crunching data to find cases such as where someone or something with characteristic X is more likely to have characteristic Y, allowing you to predict that having characteristic X makes you more likely to have characteristic Y, even though you don't understand any causal relation between the two."
   
3. "The three-dimensional structure of the more complex proteins cannot be reliably predicted from their amino acid sequence."
   

Returning to the first two posts in this thread:



In fairness to you, @sbu, I have found somebody who makes the sort of proposal you suggest: Mark Mahin of the Future and Cosmos blog. He has a set of blog posts which deal in protein folding, accessible via the "protein folding" label. I've read the first two that currently show up under that label, the first of which, Misleading Statements in a Recent Nobel Prize Announcement, directly addresses this Nobel Prize.

Based on what I've read in those two posts, Mark contends that the natural shape of proteins is not determined by the genes that code for it. He offers several reasons in support of this contention, including that:

1. Some proteins do not fold into only a single shape, but shift between shapes.
   
2. Some proteins require "chaperones" to fold into their shape.
   
3. Proteins that are "denatured" - meaning that they have lost their natural shape - do not spontaneously fold back into their natural shape.
   
4. The experiments by Christian B. Anfinsen, typically cited as proof for the hypothesis that genes determine final protein shape, were conducted on smaller proteins than average, have anyway failed replication, and are generally of dubious merit.
   
5. The main hypothesis according to which proteins spontaneously fold into their natural shape - i.e., that they strive to minimise the Gibbs free energy of the whole system - fails for a variety of reasons, including that a "search" through the possible energy states would take vast orders of magnitude longer than it actually takes proteins to fold.
   

Regarding the AlphaFold2 programme for which Dennis Hassabis and John M. Jumper won the Nobel Prize, he contends in that first article (linked above), that:

1. AlphaFold2 does not provide any insight into the supposed means by which proteins achieve their three-dimensional structures.
   
2. AlphaFold2, instead, is merely using frequentist prediction: "crunching data to find cases such as where someone or something with characteristic X is more likely to have characteristic Y, allowing you to predict that having characteristic X makes you more likely to have characteristic Y, even though you don't understand any causal relation between the two."
   
3. "The three-dimensional structure of the more complex proteins cannot be reliably predicted from their amino acid sequence."
   

I read Mark’s post and he is probably right in his critique. We don’t really understand protein folding. My only argument is that the space of foldinga given input parameters is apparently not particulary big if it can be captured by an AI model.