SearcharxivSearch

arXiv subjects

Tsvi Tlusty

Publications and source records attributed to Tsvi Tlusty.

At least 19 recordsLinked to original sources

Evolutionary modelling reveals melodic and harmonic constraints on global scale structure

Since antiquity, musical scales have been explained by harmony rather than melody. This view relies on the mathematically designed scales of a few traditions, and was never directly tested. Testing it requires cross-cultural data and a method that judges theories by what they get wrong as well as right. We provide both, modelling scale evolution across 1,314 scales from 96 countries. A Melody model explains the near-universal preference for step-sizes of 1-3 semitones, and matches independent data from melodies, singing, and psychoacoustics. Harmony does far less: it explains the music-theoretic scales, but in those measured from performance it adds only a weak bias towards fourths, fifths, and octaves. Harmony's importance has been overstated, likely due to the historical focus on music-theoretic rather than measured scales. Melody is the primary driver of global scale structure; harmonic constraints are less impactful and mainly reflect musicological theory over musical performance.

cs.SD

Resonant Untrapping of Active Polymers in Breathing Lattices

In crowded environments, active polymers can trap themselves by winding into long-lived conformations. We show that fluctuations of the surrounding confinement can resonantly accelerate escape from these self-generated traps. Brownian dynamics simulations of a driven semiflexible chain in a breathing obstacle lattice reveal intermittent switching between a compact rotating spiral and an extended translating state. Long-time diffusion increases by up to two orders of magnitude when the environmental fluctuation rate becomes comparable to the spiral's intrinsic relaxation rate. The enhancement persists under stochastic fluctuations, showing that coherent periodic forcing is not required. Activity creates a second optimum: it promotes escape once favorable conformations form, yet at strong drive stabilizes the spiral and suppresses their formation. Resonant untrapping thus provides a general mechanism by which fluctuating environments regulate transport through barriers generated by internal conformational dynamics.

cond-mat.soft

Geometric-Chemical Distance Between Protein Surfaces

Proteins recognize, bind, and catalyze through molecular surfaces, where geometry and chemical patterning determine interaction. Comparing these surfaces requires both a geometric--chemical distance and a correspondence that relates one complete surface to another. Here we introduce IFACE (Intrinsic Field--Aligned Coupled Embedding). IFACE derives a symmetric geometric--chemical distance by optimizing a probabilistic coupling over intrinsic geometry, mean curvature, electrostatics, hydrophobicity, and hydrogen-bond propensity. The same coupling provides an explicit surface map. For molecular-dynamics conformers, IFACE distinguishes the same protein from distinct proteins more accurately than TM-distance and a Laplace--Beltrami spectral distance. A Jensen--Shannon distribution distance performs best in this binary identity test, because aggregate surface-feature distributions already identify each protein. A distance must also satisfy a global requirement: its pairwise values must place many distinct protein surfaces consistently in one space. We therefore tested IFACE across six protein families. It produces the strongest family classification and clustering among the distributional, spectral, MaSIF, and SurfaceID comparisons. The inferred maps preserve geodesic neighborhoods and transfer heme-centered pocket regions across cytochrome P450 proteins. IFACE therefore provides, from one construction, both a distance between complete protein surfaces and the local map that explains that distance.

q-bio.BM

Water and the Many-Body Imagination

An electron crosses the cold Fermi sea. The sea recoils, screens, remembers. It returns the electron dressed: a quasiparticle with a mass, a lifetime, and a Green function. This was Nozières' lesson. We carry it to water. Electrons become dipoles; the Fermi sea becomes a hydrogen-bonded polar liquid. We ask the same question: can the collective modes of water live long enough and reach far enough for molecular machines to interact and synchronize?

physics.bio-ph

Interplay of Fidelity and Diversity in the Evolution of the Genetic Code

The origin and organizing principles of the genetic code remain fundamental puzzles in life science. The vanishingly low probability of the natural codon-to-amino acid mapping arising by chance has spurred the hypothesis that its structure is a solution optimized for robustness against mutations and translational errors. For the construction of effective molecular machines, the dictionary of encoded amino acids must also be diverse enough in physicochemical features. Here, we examine whether the standard genetic code can be understood as a near-optimal solution balancing these two objectives: minimizing error load and aligning codon assignments with the naturally occurring amino acid composition. Using simulated annealing, we explore this trade-off across a broad range of parameters. We find that the standard genetic code lies near local optima within the multidimensional parameter space. It is a highly effective solution that balances fidelity against resource availability constraints. These results suggest that the present genetic code reflects coevolution under conflicting pressures of fidelity and diversity, offering new insight into its emergence and evolution.

q-bio.OT

Walks in Rotation Spaces Return Home when Doubled and Scaled

The dynamics of numerous physical systems, such as spins and qubits, can be described as a series of rotation operations, i.e., walks in the manifold of the rotation group. A basic question with practical applications is how likely and under what conditions such walks return to the origin (the identity rotation), which means that the physical system returns to its initial state. In three dimensions, we show that almost every walk in SO(3) or SU(2), even a very complicated one, will preferentially return to the origin simply by traversing the walk twice in a row and uniformly scaling all rotation angles. We explain why traversing the walk only once almost never suffices to return, and comment on the problem in higher dimensions.

cond-mat.stat-mech

Information and motor constraints shape melodic diversity across cultures

The number of possible melodies is unfathomably large, yet despite this virtually unlimited potential for melodic variation, melodies from different societies can be surprisingly similar. The motor constraint hypothesis accounts for certain similarities, such as scalar motion and contour shape, but not for other major common features, such as repetition, song length, and scale size. Here we investigate the role of information constraints in shaping these hallmarks of melodies. We measure determinants of information rate in 62 corpora of Folk melodies spanning several continents, finding multiple trade-offs that all act to constrain the information rate across societies. By contrast, 39 corpora of Art music from Europe (including Turkey) show longer, more complex melodies, and increased complexity over time, suggesting different cultural-evolutionary selection pressures in Art and Folk music, possibly due to the use of written versus oral transmission. Our parameter-free model predicts the empirical scale degree distribution using information constraints on scalar motion, melody length, and, most importantly, information rate. These results provide strong evidence that information constraints during cultural transmission of music limit the number of notes in a scale, and suggests that a tendency for intermediate melodic complexity reflects a fundamental constraint on the cultural evolution of melody.

cs.SD

Statistical Survey of Chemical and Geometric Patterns on Protein Surfaces as a Blueprint for Protein-mimicking Nanoparticles

Despite recent breakthroughs in understanding how protein sequence relates to structure and function, considerably less attention has been paid to the general features of protein surfaces beyond those regions involved in binding and catalysis. This paper provides a systematic survey of the universe of protein surfaces and quantifies the sizes, shapes, and curvatures of the positively/negatively charged and hydrophobic/hydrophilic surface patches as well as correlations between such patches. It then compares these statistics with the metrics characterizing nanoparticles functionalized with ligands terminated with positively and negatively charged ligands. These particles are of particular interest because they are also surface-patchy and have been shown to exhibit both antibiotic and anticancer activities - via selective interactions against various cellular structures - prompting loose analogies to proteins. Our analyses support such analogies in several respects (e.g., patterns of charged protrusions and hydrophobic niches similar to those observed in proteins), although there are also significant differences. Looking forward, this work provides a blueprint for the rational design of synthetic nanoobjects with further enhanced mimicry of proteins' surface properties.

q-bio.BM

AI-predicted protein deformation encodes energy landscape

AI algorithms have proven to be excellent predictors of protein structure, but whether and how much these algorithms can capture the underlying physics remains an open question. Here, we aim to test this question using the Alphafold2 (AF) algorithm: We use AF to predict the subtle structural deformation induced by single mutations, quantified by strain, and compare with experimental datasets of corresponding perturbations in folding free energy $ΔΔG$. Unexpectedly, we find that physical strain alone -- without any additional data or computation -- correlates almost as well with $ΔΔG$ as state-of-the-art energy-based and machine-learning predictors. This indicates that the AF-predicted structures alone encode fine details about the energy landscape. In particular, the structures encode significant information on stability, enough to estimate (de-)stabilizing effects of mutations, thus paving the way for the development of novel, structure-based stability predictors for protein design and evolution.

q-bio.BM

Tumbling Downhill along a Given Curve

A cylinder will roll down an inclined plane in a straight line. A cone will roll around a circle on that plane and then will stop rolling. We ask the inverse question: For which curves drawn on the inclined plane $\mathbb{R}^2$ can one carve a shape that will roll downhill following precisely this prescribed curve and its translationally repeated copies? This simple question has a solution essentially always, but it turns out that for most curves, the shape will return to its initial orientation only after crossing a few copies of the curve - most often two copies will suffice, but some curves require an arbitrarily large number of copies.

math-ph

The Physical Logic of Protein Machines

Proteins are intricate molecular machines whose complexity arises from the heterogeneity of the amino acid building blocks and their dynamic network of many-body interactions. These nanomachines gain function when put in the context of a whole organism through interaction with other inhabitants of the biological realm. And this functionality shapes their evolutionary histories through intertwined paths of selection and adaptation. Recent advances in machine learning have solved the decades-old problem of how protein sequence determines their structure. However, the ultimate question regarding the basic logic of protein machines remains open: How does the collective physics of proteins lead to their functionality? and how does a sequence encode the full range of dynamics and chemical interactions that facilitate function? Here, we explore these questions within a physical approach that treats proteins as mechano-chemical machines, which are adapted to function via concerted evolution of structure, motion, and chemical interactions.

q-bio.BM

AlphaFold2 can predict single-mutation effects

AlphaFold2 (AF) is a promising tool, but is it accurate enough to predict single mutation effects? Here, we report that the localized structural deformation between protein pairs differing by only 1-3 mutations -- as measured by the effective strain -- is correlated across \num{3901} experimental and AF-predicted structures. Furthermore, analysis of ${\sim} 11000$ proteins shows that the local structural change correlates with various phenotypic changes. These findings suggest that AF can predict the range and magnitude of single-mutation effects on average, and we propose a method to improve precision of AF predictions and to indicate when predictions are unreliable.

q-bio.BM

Renormalization Group-Motivated Learning

We introduce an RG-inspired coarse-graining for extracting the collective features of data. The key to successful coarse-graining lies in finding appropriate pairs of data sets. We coarse-grain the two closest data in a regular real-space RG in a lattice while considers the overall information loss in momentum-space RG. Here we compromise the two measures for the non-spatial data set. For weakly correlated data close to Gaussian, we use the correlation of data as a metric for the proximity of data points, but minimize an overall projection error for optimal coarse-graining steps. It compresses the data to maximize the correlation between the two data points to be compressed while minimizing the correlation between the paired data and other data points. We show that this approach can effectively reduce the dimensionality of the data while preserving the essential features. We extend our method to incorporate non-linear features by replacing correlation measures with mutual information. This results in an information-bottleneck-like trade-off: maximally compress the data while preserving the information among the compressed data and the rest. Indeed, our approach can be interpreted as an exact form of information-bottleneck-like trade off near linear data. We examine our method with random Gaussian data and the Ising model to demonstrate its validity and apply glass systems. Our approach has potential applications in various fields, including machine learning and statistical physics.

physics.data-an

Convergent evolution in a large cross-cultural database of musical scales

Scales, sets of discrete pitches that form the basis of melodies, are thought to be one of the most universal hallmarks of music. But we know relatively little about cross-cultural diversity of scales or how they evolved. To remedy this, we assemble a cross-cultural database (Database of Musical Scales: DaMuSc) of scale data, collected over the past century by various ethnomusicologists. Statistical analyses of the data highlight that certain intervals (e.g., the octave, fifth, second) are used frequently across cultures. Despite some diversity among scales, it is the similarities across societies which are most striking - most scales are found close to equidistant 5- and 7-note scales. We discuss the mechanisms of variation and selection in the evolution of scales, and how the assembled data may be used to examine the root causes of convergent evolution.

physics.soc-ph

Bona fide stochastic resonance under nonGaussian active fluctuations

We report on the experimental observation of stochastic resonance (SR) in a nonGaussian active bath without any periodic modulation. A Brownian particle hopping in a nanoscale double-well potential under the influence of nonGaussian correlated noise, with mean interval ${{τ}_{P}}$ and correlation time ${{τ}_{c}}$, shows a series of equally-spaced peaks in the residence time distribution at integral multiples of ${{τ}_{P}}$. The strength of the first peak is found to be maximum when the mean residence time ${\bar{τ}_{d}}$ matches the double condition, $4{{τ}_{c}}\approx {{τ}_{P}}\approx {\bar{τ}_{d}}\text{/}2$, demonstrating a new type of bona fide SR. The experimental findings agree with a simple model that explains the emergence of SR without periodic modulation of the double-well potential. Additionally, we show that generic SR under periodic modulation, known to degrade in strongly correlated continuous noise, is recovered by the discrete nonGaussian kicks.

cond-mat.stat-mech

Gauging nanoswimmer dynamics via the motion of large bodies

Nanoswimmers are ubiquitous in bio- and nano-technology but are extremely challenging to measure due to their minute size and driving forces. A simple method is proposed for detecting the elusive physical features of nanoswimmers by observing how they affect the motion of much larger, easily traceable particles. Modeling the swimmers as hydrodynamic force dipoles, we find direct, easy-to-calibrate relations between the observable power spectrum and diffusivity of the tracers and the dynamic characteristics of the swimmers: their force dipole moment and correlation times.

physics.bio-ph

General theory of specific binding: insights from a genetic-mechano-chemical protein model

Proteins need to selectively interact with specific targets among a multitude of similar molecules in the cell. But despite a firm physical understanding of binding interactions, we lack a general theory of how proteins evolve high specificity. Here, we present such a model that combines chemistry, mechanics and genetics, and explains how their interplay governs the evolution of specific protein-ligand interactions. The model shows that there are many routes to achieving molecular discrimination - by varying degrees of flexibility and shape/chemistry complementarity - but the key ingredient is precision. Harder discrimination tasks require more collective and precise coaction of structure, forces and movements. Proteins can achieve this through correlated mutations extending far from a binding site, which fine-tune the localized interaction with the ligand. Thus, the solution of more complicated tasks is enabled by increasing the protein size, and proteins become more evolvable and robust when they are larger than the bare minimum required for discrimination. The model makes testable, specific predictions about the role of flexibility and shape mismatch in discrimination, and how evolution can independently tune affinity and specificity. Thus, the proposed theory of specific binding addresses the natural question of "why are proteins so big?". A possible answer is that molecular discrimination is often a hard task best performed by adding more layers to the protein.

q-bio.BM

Spontaneous Chiral Symmetry Breaking in a Random Driven Chemical System

Living systems have evolved to efficiently consume available energy sources using an elaborate circuitry of chemical reactions which, puzzlingly, bear a strict restriction to asymmetric chiral configurations. While autocatalysis is known to promote such chiral symmetry breaking, whether a similar phenomenon may also be induced in a more general class of configurable chemical systems -- via energy exploitation -- is a sensible yet underappreciated possibility. This work examines this question within a model of randomly generated complex chemical networks. We show that chiral symmetry breaking may occur spontaneously and generically by harnessing energy sources from external environmental drives. Key to this transition are intrinsic fluctuations of achiral-to-chiral reactions and tight matching of system configurations to the environmental drives, which together amplify and sustain diverged enantiomer distributions. These asymmetric states emerge through steep energetic transitions from the corresponding symmetric states and sharply cluster as highly-dissipating states. The results thus demonstrate a generic mechanism in which energetic drives may give rise to homochirality in an otherwise totally symmetrical environment, and from an early-life perspective, might emerge as a competitive, energy-harvesting advantage.

physics.chem-ph