Toolkit/elastic network model

elastic network model

Computational Method·Research·Since 2017

Also known as: ENM

Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

The elastic network model (ENM) is a computational method for analyzing protein structural dynamics from an elastic network representation. In the cited PAS domain superfamily study, ENM was used to quantify residue fluctuations and vibrational patterns and to relate these dynamic features to sequence conservation, structural features, and biological function.

Usefulness & Problems

Why this is useful

ENM is useful for extracting protein dynamic information from structure-based models and for comparing fluctuation patterns across related protein groups. In the cited work, it enabled analysis of how PAS domain dynamics align with conserved residues and functional classification.

Source:

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function

Source:

The result showed that the proteins with same function could be grouped by sequence similarity

Problem solved

This method helps address the problem of linking protein sequence and structure to functional evolution through dynamics. In the PAS domain study, it was applied to identify whether conserved residues and distinct functional groups exhibit characteristic fluctuation and vibrational signatures.

Taxonomy & Function

Primary hierarchy

Technique Branch

Method: A concrete computational method used to design, rank, or analyze an engineered system.

Target processes

No target processes tagged yet.

Implementation Constraints

The available evidence states that protein dynamics were analyzed using an elastic network model, implying a structure-based computational workflow rather than an experimental reagent. The provided material does not specify software implementation, parameterization, input structure requirements, or integration with other modeling steps.

The supplied evidence supports ENM use in a PAS domain superfamily analysis but does not provide broader benchmarking, predictive accuracy metrics, or comparisons to alternative dynamics methods. Practical performance characteristics, parameter sensitivity, and generalizability beyond this study are not described in the provided evidence.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 2conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 3conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 4conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 5conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 6conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 7conserved residue dynamicssupports2017Source 1needs review

Across the three PAS functional groups, residues conserved by sequence and structure analyses generally had lower fluctuation than other residues.

in all three functional groups, conserved amino acid residues identified by sequence and structure conservation analysis generally have a lower fluctuation than other residues
Claim 8dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 9dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 10dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 11dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 12dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 13dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 14dynamics difference across functional groupssupports2017Source 1needs review

Different PAS functional groups displayed statistically significant differences in vibrational patterns.

proteins in different functional groups displayed statistically significant difference in their vibrational patterns
Claim 15functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 16functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 17functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 18functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 19functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 20functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 21functional groupingsupports2017Source 1needs review

Within the PAS domain superfamily, proteins with the same function could be grouped by sequence similarity.

The result showed that the proteins with same function could be grouped by sequence similarity
Claim 22function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 23function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 24function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 25function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 26function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 27function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 28function dynamics correlationsupports2017Source 1needs review

In each PAS biological function group, fluctuation of conserved residues was strongly correlated with the corresponding biological function.

the fluctuation of conserved residues in each biological function group was strongly correlated with the corresponding biological function
Claim 29sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 30sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 31sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 32sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 33sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 34sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics
Claim 35sequence structure dynamics function connectionsupports2017Source 1needs review

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics

Approval Evidence

1 source1 linked approval claimfirst-pass slug elastic-network-model
The protein dynamics were analyzed using elastic network model (ENM)

Source:

sequence structure dynamics function connectionsupports

The study suggests a direct connection in which protein sequences are related to functions through structural dynamics.

This research suggested a direct connection in which the protein sequences were related to various functions through structural dynamics

Source:

Comparisons

Source-backed strengths

The cited study reports that residues conserved by sequence and structure analyses generally had lower fluctuation than other residues across three PAS functional groups. It also found statistically significant differences in vibrational patterns among PAS functional groups and a strong correlation between conserved-residue fluctuation and biological function within each group.

Ranked Citations

  1. 1.
    StructuralSource 1Protein Science2017Claim 1Claim 2Claim 3

    Extracted from this source document.