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

Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility.

Proceedings of the National Academy of Sciences of the United States of America - 30 Dec 2008

Tomatis Pablo E, Fabiane Stella M, Simona Fabio, Carloni Paolo, Sutton Brian J, Vila Alejandro J

Abstract excerpt

Protein evolution is crucial for organismal adaptation and fitness. This process takes place by shaping a given 3-dimensional fold for its particular biochemical function within the metabolic requirements and constraints of the environment. The complex interplay between sequence, structure, functionality, and stability that gives rise to a particular phenotype has limited the identification of traits acquired...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus cereus
Share to beta-Lactamases

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

Share to Catalysis

Share to Directed Molecular Evolution

Share to Drug Resistance, Bacterial

Share to Enzyme Stability

Share to Epistasis, Genetic

Share to Metalloproteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19098096
DOI: 10.1073/pnas.0807989106
PMCID: PMC2634896

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

Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility.PMID 19098096Read ↗

Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Semantic proximity Read ↗

Evolution of β-lactamases and enzyme promiscuitySemantic proximity Read ↗

Capturing the mutational landscape of the beta-lactamase TEM-1.Semantic proximity Read ↗

Negative Epistasis and Evolvability in TEM-1 β-Lactamase--The Thin Line between an Enzyme's Conformational Freedom and Disorder.Semantic proximity Read ↗

Insights into an evolutionary strategy leading to antibiotic resistance.Semantic proximity Read ↗

Environmental selection and epistasis in an empirical phenotype-environment-fitness landscape.Semantic proximity Read ↗

Rapid evolutionary change in trait correlations of single proteins.Semantic proximity Read ↗

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

Network of epistatic interactions in an enzyme active site revealed by large-scale deep mutational scanning.Semantic proximity Read ↗

Higher-order epistasis drives evolutionary unpredictability toward novel antibiotic resistanceSemantic proximity Read ↗

Understanding epistatic networks in the B1 β-lactamases through coevolutionary statistical modeling and deep mutational scanning.Semantic proximity Read ↗

Single-mutation fitness landscapes for an enzyme on multiple substrates reveal specificity is globally encoded.Semantic proximity Read ↗

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