Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A biophysical protein folding model accounts for most mutational fitness effects in viruses.

Proceedings of the National Academy of Sciences of the United States of America - 14 Jun 2011

Wylie C Scott, Shakhnovich Eugene I

Abstract excerpt

Fitness effects of mutations fall on a continuum ranging from lethal to deleterious to beneficial. The distribution of fitness effects (DFE) among random mutations is an essential component of every evolutionary model and a mathematical portrait of robustness. Recent experiments on five viral species all revealed a characteristic bimodal-shaped DFE featuring peaks at neutrality and lethality. However, the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Algorithms
Share to Biological Evolution
Share to Models, Chemical

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Population Density

Share to Protein Folding

Share to Thermodynamics

Share to Viral Proteins

Share to Viruses

Source

Open in PubMed Open full text

Identifiers

PMID: 21610162
DOI: 10.1073/pnas.1017572108
PMCID: PMC3116435

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A biophysical protein folding model accounts for most mutational fitness effects in viruses.PMID 21610162Read ↗

Lethal mutagenesis in viruses and bacteria.Semantic proximity Read ↗

Estimating the contribution of folding stability to nonspecific epistasis in protein evolution.Semantic proximity Read ↗

Biophysical fitness landscape design traps viral evolutionSemantic proximity Read ↗

Interactions between evolutionary processes at high mutation rates.Semantic proximity Read ↗

Mutational and fitness landscapes of an RNA virus revealed through population sequencing.Semantic proximity Read ↗

Protein stability imposes limits on organism complexity and speed of molecular evolution.Semantic proximity Read ↗

Evolutionary dynamics of viral escape under antibodies stress: A biophysical model.Semantic proximity Read ↗

Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein.Semantic proximity Read ↗

Atomistic simulation of protein evolution reveals sequence covariation and time-dependent fluctuations of site-specific substitution rates.Semantic proximity Read ↗

Mutation bias favors protein folding stability in the evolution of small populations.Semantic proximity Read ↗

Mutation induced extinction in finite populations: lethal mutagenesis and lethal isolation.Semantic proximity Read ↗

Evolution favors protein mutational robustness in sufficiently large populations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.