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Related Experiment Video

Updated: Jun 24, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Protein dynamism and evolvability.

Nobuhiko Tokuriki¹, Dan S Tawfik

¹Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

Science (New York, N.Y.)

|April 11, 2009

Summary

This summary is machine-generated.

Proteins are dynamic and adaptable, not fixed. This flexibility and functional promiscuity are key to protein evolution, enabling new functions and structures.

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Area of Science:

Biochemistry
Molecular Biology
Evolutionary Biology

Background:

Traditional view: proteins have fixed structures and specific functions.
Observation: proteins demonstrate remarkable adaptability and evolution of new functions/structures.
Conflict: fixed structure/function model versus observed protein plasticity.

Purpose of the Study:

Propose an alternative "avant-garde view" of protein structure and function.
Explore the role of protein dynamism and functional promiscuity in protein evolvability.
Investigate the impact of protein packing on evolvability.

Main Methods:

Conceptual framework development based on existing literature.
Analysis of protein conformational dynamics and functional promiscuity.
Extrapolation of dynamic principles to early protein evolution and future research.

Main Results:

Proteins are conformationally dynamic and functionally promiscuous.
These properties are foundational to protein evolvability.
Poorly packed and disordered proteins exhibit higher evolvability.
Dynamic view facilitates understanding of new function/fold evolution.

Conclusions:

Protein dynamism and functional promiscuity are central to protein evolution.
Understanding protein dynamics is crucial for predicting evolutionary trajectories.
Future research should focus on protein dynamism and its evolutionary implications.