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 perturbative view of protein structural variation.

Proteins - 1 Jan 2010

Echave Julián, Fernández Francisco M

Abstract excerpt

It was recently found that the lowest-energy collective normal modes dominate the evolutionary divergence of protein structures. This was attributed to a presumed functional importance of such motions, i.e., to natural selection. In contrast to this selectionist explanation, we proposed that the...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Databases, Protein
Share to Evolution, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Globins

Share to Models, Genetic

Share to Myoglobin

Share to Protein Conformation

Share to Whales

Source

Identifiers

PMID: 19731380
DOI: 10.1002/prot.22553

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-19731380-2026-09-04.1. Manifest publication-graph-cohort-2026-09-04.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A perturbative view of protein structural variation.PMID 19731380Read ↗

Global Dynamics Renders Protein Sites with High Functional Response.Semantic proximity Read ↗

Mutation-induced reshaping of protein conformational dynamics revealed by a coarse-grained modeling frameworkSemantic proximity Read ↗

Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?Semantic proximity Read ↗

Rapid Characterization of Allosteric Networks with Ensemble Normal Mode Analysis.Semantic proximity Read ↗

A coarse-grained elastic network atom contact model and its use in the simulation of protein dynamics and the prediction of the effect of mutations.Semantic proximity Read ↗

Protein as evolvable functionally constrained amorphous matter.Semantic proximity Read ↗

A General Mechanism for the Propagation of Mutational Effects in Proteins.Semantic proximity Read ↗

Dynamics-Evolution Correspondence in Protein Structures.Semantic proximity Read ↗

Green function of correlated genes in a minimal mechanical model of protein evolution.Semantic proximity Read ↗

The Role of Conformational Dynamics and Allostery in the Disease Development of Human Ferritin.Semantic proximity Read ↗

Molecular model of human tropoelastin and implications of associated mutations.Semantic proximity Read ↗

Evolutionary pathways in epistatic mechanical networks.Semantic proximity Read ↗

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