en.wikipedia.org/wiki/There%27s_Plenty_of_Room_at_the_Bottom
2 corrections found
Such protein domain dynamics can only now be seen by neutron spin echo spectroscopy.
This is too absolute: protein and ribosome conformational dynamics have been observed with several other methods, including NMR, cryo-EM, and single-molecule FRET.
Full reasoning
The sentence says these dynamics can only be seen by neutron spin echo spectroscopy, but the literature shows otherwise.
- A 2013 review in Progress in Biophysics and Molecular Biology states that "The contemporary methods of NMR spectroscopy are capable to provide the detailed information on domain motions in biomacromolecules" and reviews domain motions across biomacromolecules measured by NMR.
- A 2008 Molecular Cell paper reports, "using single-molecule FRET, we observe that pretranslocation ribosomes undergo spontaneous intersubunit rotational movement"—i.e., ribosome conformational dynamics were directly observed with smFRET.
- An NCBI Bookshelf review on ribosomes says that structural changes in the ribosome "have been observed using a variety of techniques over the years", specifically naming cryoelectron microscopy and x-ray crystallography in addition to other approaches.
Because multiple well-established techniques besides neutron spin echo spectroscopy have been used to observe protein/ribosome domain dynamics, the article's exclusive wording is incorrect.
3 sources
- NMR spectroscopy on domain dynamics in biomacromolecules - PubMed
"The contemporary methods of NMR spectroscopy are capable to provide the detailed information on domain motions in biomacromolecules in the wide range of timescales related to the timescales of their functioning."
- Spontaneous intersubunit rotation in single ribosomes - PubMed
"Here, using single-molecule FRET, we observe that pretranslocation ribosomes undergo spontaneous intersubunit rotational movement..."
- Conformational Dynamics within the Ribosome - NCBI Bookshelf
"Individual structural changes in the ribosome ... have been observed using a variety of techniques over the years. With new high resolution cryoelectron microscopy and x-ray crystallography structure models available..."
This text uses exactly 1 kibibyte, i.e., 8192 bits, made with 1 atom vacancy each, constituting thereby the first atomic kibibyte, with a storage density 500 times larger than the state of the art approaches.
The underlying TU Delft/Nature paper describes the device as a 1 kilobyte memory with 8,000 bits, not a 1 kibibyte memory with 8,192 bits.
Full reasoning
The article's bit-count terminology is wrong.
The 2016 Nature Nanotechnology paper behind this experiment describes the device as "up to 1 kilobyte (8,000 bits)". TU Delft's own repository repeats the same wording, and OtteLab's later summary says the memory stored 8,000 bits with one atom per bit. A kibibyte is 1,024 bytes = 8,192 bits, which is different.
So while the article is broadly referring to the same atomic-memory demonstration, the specific claim that the stored text used exactly 1 kibibyte (8192 bits) is contradicted by the researchers' own description of the device as 1 kilobyte / 8,000 bits.
3 sources
- A kilobyte rewritable atomic memory | TU Delft Repository
"Here, we present a robust digital atomic-scale memory of up to 1 kilobyte (8,000 bits) using an array of individual surface vacancies..."
- A kilobyte rewritable atomic memory - arXiv
"Here we present a robust digital atomic scale memory of up to 1 kilobyte (8,000 bits)..."
- OtteLab | Media
"In 2016... we demonstrated the possibility to store a full kilobyte of data in a device where each of the 8,000 bits is represented by the position of a single atom."