Lifeboat Foundation

The Schwartz Reisman Institute for Technology and Society and the Department of Computer Science at the University of Toronto, in collaboration with the Vector Institute for Artificial Intelligence and the Cosmic Future Initiative at the Faculty of Arts \& Science, present Geoffrey Hinton on October 27, 2023, at the University of Toronto.

0:00:00 — 0:07:20 Opening remarks and introduction.
0:07:21 — 0:08:43 Overview.
0:08:44 — 0:20:08 Two different ways to do computation.
0:20:09 — 0:30:11 Do large language models really understand what they are saying?
0:30:12 — 0:49:50 The first neural net language model and how it works.
0:49:51 — 0:57:24 Will we be able to control super-intelligence once it surpasses our intelligence?
0:57:25 — 1:03:18 Does digital intelligence have subjective experience?
1:03:19 — 1:55:36 Q\&A
1:55:37 — 1:58:37 Closing remarks.

Continue reading “Will digital intelligence replace biological intelligence?” »

A critical molecule for the metabolism of living organisms has been synthesized for the first time by University of Hawaiʻi at Mānoa researchers at low temperatures (10 K) on ice coated nanoparticles mimicking conditions in deep space, marking a “cool” step in advancing our understanding of the origins of life.

Engineers have unveiled an encodable multifunctional material that can dynamically tune its shape and mechanical properties in real time. Inspired by the remarkable adaptability observed in biological organisms like the octopus, a breakthrough has been achieved in soft machines. A research team, led by Professor Jiyun Kim in the Department of Materials Science and Engineering at UNIST has successfully developed an encodable multifunctional material that can dynamically tune its shape and mechanical properties in real-time. This groundbreaking metamaterial surpasses the limitations of existing materials, opening up new possibilities for applications in robotics and other fields requiring adaptability.

Current soft machines lack the level of adaptability demonstrated by their biological counterparts, primarily due to limited real-time tunability and restricted reprogrammable space of properties and functionalities.

In order to bridge this gap, the research team introduced a novel approach utilizing graphical stiffness patterns.

Organic materials discovered on Mars may have originated from atmospheric formaldehyde, according to new research, marking a step forward in our understanding of the possibility of past life on the Red Planet.

Scientists from Tohoku University have investigated whether the early atmospheric conditions on Mars had the potential to foster the formation of biomolecules – organic compounds essential for biological processes.

Their findings, published in Scientific Reports, offer intriguing insights into the plausibility of Mars harboring life in its distant past.

Drawing inspiration from the extraordinary adaptability seen in biological entities such as the octopus, a significant advancement in the field of soft robotics has been made. Under the guidance of Professor Jiyun Kim from the Department of Materials Science and Engineering at UNIST, a research team has successfully developed an encodable multifunctional material that can dynamically tune its shape and mechanical properties in real-time.

This groundbreaking metamaterial surpasses the limitations of existing materials, opening up new possibilities for applications in robotics and other fields requiring adaptability.

Current soft machines lack the level of adaptability demonstrated by their biological counterparts, primarily due to limited real-time tunability and restricted reprogrammable space of properties and functionalities. In order to bridge this gap, the research team introduced a novel approach utilizing graphical stiffness patterns. By independently switching the digital binary stiffness states (soft or rigid) of individual constituent units within a simple auxetic structure featuring elliptical voids, the material achieves in situ and gradational tunability across various mechanical qualities.

The FIT4NANO project has mapped out the expansive applications and future directions of focused ion beam technology, emphasizing its critical role in advancing research and development across multiple disciplines, from microelectronics to life sciences.

Processing materials on the nanoscale, producing prototypes for microelectronics, or analyzing biological samples: The range of applications for finely focused ion beams is huge. Experts from the EU collaboration FIT4NANO have now reviewed the many options and developed a roadmap for the future. The article, published in Applied Physics Review, is aimed at students, users from industry and science as well as research policymakers.

Discovery and Applications.

The motions within the molecule provide a new way to compare the structures and functions of similar proteins.

Proteins play a central role in nearly every biological process, and they often change shape as they function. Over the past decade, a research team has developed a method of analysis that can help make sense of the available atomic-scale structural data and reveal the key physical distortions that underlie protein functions. Now the team has shown that the technique provides a consistent way of comparing proteins from different species, demonstrating similar structural changes in many of them [1]. The researchers believe that the technique will help biologists better understand the cross-species variations among proteins.

Proteins are linear chains of amino acids that fold up into specific three-dimensional shapes. Although there are lots of atomic-scale data on the structural changes that protein molecules execute as they function, researchers have had few quantitative methods to extract insights from these data, says biophysicist Pablo Sartori of the Gulbenkian Institute of Science in Portugal. One challenge, he says, is the arbitrary choice one makes when comparing two similar protein structures, such as the structures of a protein in two different conformations. “If you align region A of the protein, then region B shows displacement. If you align region B, then region A shows displacement. If you align the average, then both are displaced a bit.” Another problem is that the relative displacement is often not the quantity that best reflects the structural changes associated with protein function.

The perplexing phenomenon of homochirality in life, where biomolecules exist in only one of two mirror-image forms, remains unexplained despite historical attention from scientific figures like Pasteur, Lord Kelvin, and Pierre Curie. Recent research suggests the combination of electric and magnetic fields might influence this preference through experiments showing enantioselective effects on chiral molecules interacting with magnetized surfaces, offering indirect evidence towards understanding this mystery.

The phenomenon known as homochirality of life, which refers to the exclusive presence of biomolecules in one of their two possible mirror-image configurations within living organisms, has intrigued several prominent figures in science. This includes Louis Pasteur, who first identified molecular chirality, William Thomson (also known as Lord Kelvin), and Pierre Curie, a Nobel Laureate.

A conclusive explanation is still lacking, as both forms have, for instance, the same chemical stability and do not differ from each other in their physicochemical properties. The hypothesis, however, that the interplay between electric and magnetic fields could explain the preference for one or the other mirror-image form of a molecule – so-called enantiomers – emerged early on.

Researchers have discovered a mechanism steering the evolution of multicellular life. They identify how altered protein folding drives multicellular evolution.

In a new study led by researchers from the University of Helsinki and the Georgia Institute of Technology, scientists turned to a tool called experimental evolution. In the ongoing Multicellularity Long Term Evolution Experiment (MuLTEE), laboratory yeast are evolving novel multicellular functions, enabling researchers to investigate how they arise.

The study, published in Science Advances, puts the spotlight on the regulation of proteins in understanding evolution.