We develop an algorithmic framework for contracting tensor networks and demonstrate its power by classically simulating quantum computation of sizes previously deemed out of reach. Our main contribution, index slicing, is a method that efficiently parallelizes the contraction by breaking it down into much smaller and identically structured subtasks, which can then be executed in parallel without dependencies. We benchmark our algorithm on a class of random quantum circuits, achieving greater than 10 times acceleration over the original estimate of the simulation cost. We then demonstrate applications of the simulation framework for aiding the development of quantum algorithms and quantum error correction. As tensor networks are widely used in computational science, our simulation framework may find further applications.
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http://dx.doi.org/10.1038/s43588-021-00119-7 | DOI Listing |
J Inorg Biochem
December 2024
Faculty of Chemistry (UPV/EHU), Manuel Lardizabal 3, Donostia-San Sebastian 20018, Spain; DIPC, Manuel Lardizabal 4, Donostia-San Sebastian 20018, Spain. Electronic address:
Mimosine, a non-essential amino acid derived from plants, has a strong affinity for binding divalent and trivalent metal cations, including Zn, Ni, Fe, and Al. This ability endows mimosine with significant antimicrobial and anti-cancer properties, making it a promising candidate for therapeutic applications. Previous research has demonstrated the effectiveness of mimosine-containing peptides as metal chelators, offering a safer alternative to conventional chelation agents.
View Article and Find Full Text PDFJ Chem Phys
December 2024
Department of Physics, Stockholm University, AlbaNova University Center, SE-10691 Stockholm, Sweden.
Vibrational polaritons are formed by strong coupling of molecular vibrations and photon modes in an optical cavity. Experiments have demonstrated that vibrational strong coupling can change molecular properties and even affect chemical reactivity. However, the interactions in a molecular ensemble are complex, and the exact mechanisms that lead to modifications are not fully understood yet.
View Article and Find Full Text PDFACS Catal
December 2024
Department of Chemistry, Michigan Technological University, Houghton, Michigan 49931, United States.
The ethylene-forming enzyme (EFE) is a Fe(II)/2-oxoglutarate (2OG) and l-arginine (l-Arg)-dependent oxygenase that primarily decomposes 2OG into ethylene while also catalyzing l-Arg hydroxylation. While the hydroxylation mechanism in EFE is similar to other Fe(II)/2OG-dependent oxygenases, the formation of ethylene is unique. Various redesign strategies have aimed to increase ethylene production in EFE, but success has been limited, highlighting the need for alternate approaches.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Key Laboratory of Forest Food Resources Utilization of Heilongjiang Province, Harbin 150040, China; College of Life Sciences, Northeast Forestry University, Harbin 150040, China. Electronic address:
The present study investigated the covalent binding behavior of the flavonoids, catechin, eriodictyol, luteolin and quercetin with β-lactoglobulin (βlg). Since the four flavonoids possess the identical A- and B-ring structures, effects of the C-rings on the properties of flavonoids and the corresponding semiquinones are revealed. Experimental methods including DLS and CD spectra indicated that with quercetin at room temperature did not induce aggregation of βlg, whilst binding with the other three flavonoids resulted in aggregation of βlg.
View Article and Find Full Text PDFJ Phys Chem B
December 2024
Department of Chemistry and Biochemistry, University of Lethbridge, 4401 University Drive West, Lethbridge, Alberta, Canada T1K 3M4.
Despite the remarkable resistance of the nucleic acid phosphodiester backbone to degradation affording genetic stability, the P-O bond must be broken during DNA repair and RNA metabolism, among many other critical cellular processes. Nucleases are powerful enzymes that can enhance the uncatalyzed rate of phosphodiester bond cleavage by up to ∼10-fold. Despite the most well accepted hydrolysis mechanism involving two metals (M to activate a water nucleophile and M to stabilize the leaving group), experimental evidence suggests that some nucleases can use a single metal to facilitate the chemical step, a controversial concept in the literature.
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