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

The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.

Proteins - 1 Apr 2016

Hoffmann Jordan, Wrabl James O, Hilser Vincent J

Abstract excerpt

Knowing the determinants of conformational specificity is essential for understanding protein structure, stability, and fold evolution. To address this issue, a novel statistical measure of energetic compatibility between sequence and structure was developed using an experimentally validated model of the energetics of the native state ensemble. This approach successfully matched sequences from a diverse subset of...

Read the complete abstract on PubMed

Topics

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

Share to Databases, Protein
Share to Genome, Human
Share to Protein Domains

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

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Proteome

Share to Selection, Genetic

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 26800099
DOI: 10.1002/prot.24989
PMCID: PMC4811355

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

The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.PMID 26800099Read ↗

Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Semantic proximity Read ↗

Evolutionarily conserved pathways of energetic connectivity in protein families.Semantic proximity Read ↗

The effect of sequence evolution on protein structural divergence.Semantic proximity Read ↗

Protein 3D structure computed from evolutionary sequence variation.Semantic proximity Read ↗

Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.Semantic proximity Read ↗

An energetic representation of protein architecture that is independent of primary and secondary structure.Semantic proximity Read ↗

Coevolution-based inference of amino acid interactions underlying protein function.Semantic proximity Read ↗

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

The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution.Semantic proximity Read ↗

Design of Protein Multi-specificity Using an Independent Sequence Search Reduces the Barrier to Low Energy SequencesSemantic proximity Read ↗

In-Silico Stability Predictors: Investigation of Performance Towards balanced Experimental DataSemantic proximity Read ↗

Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.Semantic proximity Read ↗

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