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AI cannot cure cancers.
(Fig.1) Today's medicine, hyped AI are deadend due to useless electron microscopes that cannot clarify atomic mechanisms of proteins or diseases.
Today's medical research is deadend, unable to cure diseases such as cancers, Alzheimer.. because the present medical or biological researches do Not consider or clarify atomic mechanism of proteins or diseases, contrary to hypes.
Optical microscopes often used in today's medical research cannot see atoms (= each atomic size is 0.1nm = 1Å ) due to their bad resolution (> 100nm = 0.1μm, this-3rd-paragaph ).
↑ Even if they attach different fluorescent markers to different molecules or antibodies, this fluorescent microscope's resolution is too bad to see single atoms.
Today's best methods for seeing atomic structures of proteins are X-ray crystallography, NMR and cryo-electron microscopes (= cryo-EM ).
X-ray- crystallography, which is most often used to determine proteins' structures in protein structure data band (= PDB ), is useless, unable to clarify atomic mechanism, because most proteins cannot be crystallized (= cannot be observed by X-ray crystallography ).
This-1. crystalline sample says
"The requirement for a crystalline sample is one of the most significant restrictions of x-ray crystallography....
Complex, big, or membrane-embedded proteins frequently cause them to fail, ( this-2nd-paragarph )"
And even the luckily-crystallized proteins have unreal structures different from actual dynamical structures inside cells or bodies or bad resolutions. ← cannot be used for drug discovery.
This-X-ray crystallography-4th-paragraph says
"Large, complex molecules are often difficult to crystallize, especially when they contain dynamic areas.... Finally, the crystallization process can affect the molecular structure in a manner that means the final elucidated structure could be completely different to the native one found under physiological conditions"
NMR (= nuclear magnetic resonance ) is also useless, able to see only small molecules that must be purified ( this-Disadvantage of NMR, this-p.2-4th-paragraph, this-NMR-disadvantage ).
(Fig.C) Today's best microscope = Cryo-electron microscope cannot clarify atomic mechanism. → No cure for diseases, AI is useless.
Cryo-electron microscopes (= cryo-EM ) seeing electrons randomly scattered by target proteins are also useless with bad resolution that can Not see nor clarify atomic mechanisms ( this-p.4-5 ).
↑ In the sample of cryo-EM, target (dirty) proteins often attached to various irrelevant molecules are placed and oriented randomly, which makes it impossible for the electron microscope to clearly see atomic structures of the target proteins.
This-p.11-conclusions say
"Although the current highest resolution
reached 1.2 Å, most of the reported cryo-EM structures
are still at the 3–4Å level (= cryo-EM cannot see single atoms of 1Å size ), and therefore the structural
information on drug molecule binding target sites usually needs to be combined with higher resolution protein
structures obtained from X-ray crystallography"
This-7~8th-paragraphs (2025) say
"However, cryo-EM's resolution typically doesn't match the atomic-level precision of crystallography"
This-Limitations of cryo-EM (2024) says
"There are resolution limitations and sometimes structural details cannot be well-resolved.
Larger samples are difficult to study."
Even in the latest researches in 2025, cryo-EM cannot get the atomic level resolution (< 1Å = a angstrom ), as shown in this-abstract-5.8Å resolution, this-p.5-4.33Å resolution this-p.1-3.04Å resolution, this-p.3-2.8Å resolution, this-p.3-5-3.75Å resolution
In cryo-electron microscopes, it is extremely difficult to purify homogenious proteins (= isolating only some target proteins means protein-protein interactions or enzymatic reactions cannot be clarified by cryo-EM ) = if target proteins' conformations are flexibly changed or mixed with irrelevant molecules, cryo-EM cannot precisely determine the atomic structures of proteins ( this-lower-Challenges and limitation ).
This-middle-current limitations and challeges in cryo-EM say
"Sample heterogeneity: Membrane proteins can be difficult to purify and can exist in multiple conformational states."
(Fig.P) Why today's AI, Alphafold cannot develop drugs ?
Today's microscopes unable to clarify native atomic structures is why the overhyped AI, Alphafold that are trained only on proteins structures in PDB ( this-p.2-right ) obtained by these useless X-ray crystallography, NMR, cryo-EM cannot predict real atomic structures of various proteins nor develop effective drugs.
This-1st paragraph(6/25/2025) say
"AI won't revolutionize drug discovery"
This-abstract-(12/25/2024) says
" However, despite high expectations, few AI-discovered or AI-designed drugs have entered human clinical trials, and none have achieved clinical approval."
This-p.3-right-last~p.4-left (2024) says
"It is still an open question whether the structures in a cellular environment can be truthfully reproduced by
AlphaFold2 prediction or in in vitro experiments"
This-7~8th, 10th paragraphs (5/26/2025) say
"AI oversimplifies the representation of the protein's flexible regions."
"while AI tools like AlphaFold are powerful, their training data lacks information about complex protein behavior"
This-middle-cryo-electron microscopy-2nd, 3rd, 7th~ paragaraphs (3/11/2025) say
"However, cryo-EM is not without its limitations... The images produced are averages of thousands of molecular snapshots, meaning that for highly flexible proteins, the final structure can be blurry or incomplete."
"X-ray crystallography requires proteins to be coaxed into a crystalline form,.. not all proteins crystallize well. "
"The core issue AI isn't just missing data — AlphaFold’s entire approach is built on assumptions that don't apply to disordered proteins (= related to diseases, so AI cannot cure diseases )"
(Fig.M) Useful multi-probe atomic force microscopes clarifying atomic mechanism are hampered by unreal quantum mechanical fictional atomic models.
The only method for clarifying atomic mechanism of proteins and diseases is multi-probe atomic force microscopes that can directly see and manipulate single atoms of any target proteins and cells.
Atomic force microscopes (= AFM ) are the only tool to get even subatomic (= smaller than a single atom < 1Å = 100pm ) resolution ( this-1st-paragraph, this-p.2-p.7 ).
This-p.8-right-2 says
"Subatomic spatial resolution...
to our knowledge, AFM (= atomic force microscope ) is the only tool that allows to
see structure within an atom. ..Figure 5b show subatomically resolved
images of a single atom Si tip and a W.... subatomic resolution.. observed with a CO terminated tip"
But today's useless quantum mechanical atomic theory tries to describe any molecules and proteins as fictional quasiparticles with fake mass and charge or one pseudo-electron DFT (= density functional theory ) model lacking real atomic shape.
↑ This unreal impractical quantum mechanical shapeless atomic model, DFT, extremely time-consuming molecular dynamics (= MD ) have hampered developing useful multi-probe atomic force microscopes for a long time.
Due to this current useless quantum mechanical atomic model, today's atomic force microscopes (= AFM ) with only one probe tips or multiple probes are used only to vaguely see cells or large objects without seeing nor distinguishing single atomic structures. ← Our nanotechnology is regressing ( compare this-p.7-upper and this ).
This-p.3-left-last-paragraph says
"The resolution of these methods is not
limited by the diffraction of light as in optical microscopy, but
is instead limited by the sharpness of the scanning probe,
typically 2–10 nm. However, even atomic resolution can be
achieved with an appropriate tip."
↑ So the current biological or medical researches intentionally avoid using the sharp single-atomic tips for atomic force microscopes that can get atomic resolution, because only multi-probe atomic force microscopes, whose development is hampered by unreal quantum mechanics, can see 3-dimensional atomic structures of target molecules and proteins (= it is hard for today's useless single-probe microscopes to get 3-d atomic structures, this-lower-challenges ).
So we should immediately develop useful multi-probe atomic force microscopes (= we already have this technology, but academia trying to protect the old impractical quantum mechanics has been preventing it ) controlling single atoms freely to observe and clarify detailed atomic mechanisms of proteins for curing diseases by gradually manipulating and breaking target proteins through artificial bond breaking.
(Fig.2) Overhyped news and researches claiming "atomic mechanisms of proteins and diseases were investigated" are useless, could Not clarify real atomic mechanisms at all.
Today's medical research is useless, unable to clarify atomic mechanism of diseases, because medical researches use only macroscopic biological tools such as PCR enzymes, plasmid DNA, antibodies obtained from natural organisms, which cannot see nor clarify atomic mechanisms of diseases ( this-1st-paragraph, this-p.1-abstract ).
Even overhyped news or researches on "atomic-level mechanism of diseases" do Not clarify the real atomic mechanisms ( this-p.11-conclusions and perspective ). ↓
For example, this-p.20-right-Limitations of the modeling approach says
"These are based,
respectively, on cryo-EM structures.. and X-ray structures
of prokaryotic sodium channel.... Since the experimental structures
are obtained in lack of lipid membranes and membrane voltage,
some of their features may be non-native (= unreal structures ).... Furthermore, in lack of experimental
structural data on the C-terminal part of linker I/II we refrained
from an attempt to de novo model this part"
This-lower-Next step says
"It is likely that the conformational changes we observe are controlled by yet-to-be-found regulators in cells" ← still atomic mechanisms are unclear.
(Fig.A) Overhyped fake news on seeing atomic mechanisms of cells is rampant in medical research. ↓
The 2nd-last paragraph of this hyped news on the alleged atomic level DNA transcription (2025) says
"Our findings may (= uncertain speculation, so still useless ) contribute to a better understanding of diseases"
↑ This research used cryo-EM whose resolution was very bad (= 3.0Å ~ 15Å, this-p.10-left, this-p.6~8 compared with this and this ), which cannot distinguish single atoms of 1Å size, hence No atomic mechanism was clarified, contrary to hypes.
This other hyped research on the alleged molecular mechanism of brain blood ( this paper ↓ )
p.4-Figure 1G's transmission electron microscope's picture cannot see nor distinguish single atoms (= so No atomic mechanism was clarified ).
p.12-Limitaions of the study-right-middle says
"Moreover, the
regional specificity of N-cadherin expression in the brain remains
poorly understood" ← still atomic mechanism cannot be understood, contrary to hypes.
The 1st, 6th and last paragraphs of this hyped news about "atomic interaction of cancers" say
"The successful development of a candidate therapy can often be hampered, however, by a lack of understanding about its mechanism of action at the atomic level, which is very difficult to determine experimentally"
"research team used (useless) density functional theory calculations to study the interactions between the surface of cerium oxide and various molecules"
"The theory is actually ahead of the computational power available (= only impractical quantum theory, No computation of atomic interaction ). Today we are able to model 100 atoms using fairly long-standing theory. While incredible insights are possible, this limits the scope of what you can do" ← No clarifying atomic mechanisms of cancers consisting of many atoms.
This-p.9-left (of another hyped atomic-level mechanism research ) says
" brute force unbiased MD (= molecular dynamics ) simulations,.. still remains out of reach (= MD is too time-consuming to simulate actual molecules )."
"pose many challenges even for these methods,.. Finally, MD simulations rely on
FFs (= pseudo-force field potential ), which are inherently approximated. Their limitations, and
associated uncertainties,"
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