activity
20072026
most citedInference of Co-Evolving Site Pairs: an Excellent Predictor of Contact Residue Pairs in Protein 3D structures

18 citations · 58 across the 10 of their papers we have counts for

collaborators

10 papers

q-bio.BM2026

Boltzmann Machine Learning with a Parallel, Persistent Markov chain Monte Carlo method for Estimating Evolutionary Fields and Couplings from a Protein Multiple Sequence Alignment

Sanzo Miyazawa

The inverse Potts problem for estimating evolutionary single-site fields and pairwise couplings in homologous protein sequences from their single-site and pairwise amino acid frequ…

q-bio.PE2019★ 1 cited

Boltzmann machine learning and regularization methods for inferring evolutionary fields and couplings from a multiple sequence alignment

Sanzo Miyazawa

The inverse Potts problem to infer a Boltzmann distribution for homologous protein sequences from their single-site and pairwise amino acid frequencies recently attracts a great de…

q-bio.BM2017★ 2 cited

Prediction of Structures and Interactions from Genome Information

Sanzo Miyazawa

Predicting three dimensional residue-residue contacts from evolutionary information in protein sequences was attempted already in the early 1990s. However, contact prediction accur…

q-bio.PE2016★ 16 cited

Selection originating from protein stability/foldability: Relationships between protein folding free energy, sequence ensemble, and fitness

Sanzo Miyazawa

Assuming that mutation and fixation processes are reversible Markov processes, we prove that the equilibrium ensemble of sequences obeys a Boltzmann distribution with $\exp(4N_e m(…

q-bio.PE2016

Selection originating from protein foldability: I. A new method to estimate selection temperature

Sanzo Miyazawa

The probability distribution of sequences with maximum entropy that satisfies a given amino acid composition at each site and a given pairwise amino acid frequency at each site pai…

q-bio.PE2015

Selection maintaining protein stability at equilibrium

Sanzo Miyazawa

The common understanding of protein evolution has been that neutral or slightly deleterious mutations are fixed by random drift, and evolutionary rate is determined primarily by th…