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

Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection.

Molecular systems biology - 13 Jul 2010

Peña Matthew I, Davlieva Milya, Bennett Matthew R, Olson John S, Shamoo Yousif

Abstract excerpt

Systems biology can offer a great deal of insight into evolution by quantitatively linking complex properties such as protein structure, folding, and function to the fitness of an organism. Although the link between diseases such as Alzheimer's and misfolding is well appreciated, directly showing the importance of protein folding to success in evolution has been more difficult. We show here that predicting...

Read the complete abstract on PubMed

Topics

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

Share to Adenylate Kinase
Share to Bacillus subtilis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calorimetry, Differential Scanning

Share to Enzyme Stability

Share to Genetic Fitness

Share to Geobacillus stearothermophilus

Share to Population Dynamics

Share to Systems Biology

Source

Open in PubMed Open full text

Identifiers

PMID: 20631681
DOI: 10.1038/msb.2010.43
PMCID: PMC2925523

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection.PMID 20631681Read ↗

Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.Semantic proximity Read ↗

Evolution of a single gene highlights the complexity underlying molecular descriptions of fitness.Semantic proximity Read ↗

In vivo molecular evolution reveals biophysical origins of organismal fitness.Semantic proximity Read ↗

Protein folding and binding can emerge as evolutionary spandrels through structural coupling.Semantic proximity Read ↗

An adaptive mutation in adenylate kinase that increases organismal fitness is linked to stability-activity trade-offs.Semantic proximity Read ↗

In the light of directed evolution: pathways of adaptive protein evolution.Semantic proximity Read ↗

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

The fitness challenge of studying molecular adaptation.Semantic proximity Read ↗

Diminishing returns and tradeoffs constrain the laboratory optimization of an enzyme.Semantic proximity Read ↗

Natural history as a predictor of protein evolvability.Semantic proximity Read ↗

Collateral fitness effects of mutation are not commonly caused by protein misfoldingSemantic proximity Read ↗

Stability effects of mutations and protein evolvability.Semantic proximity Read ↗

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