Moving beyond static snapshots: Protein dynamics and the Protein Data Bank

J Biol Chem. 2021 Jan-Jun:296:100749. doi: 10.1016/j.jbc.2021.100749. Epub 2021 May 4.

Abstract

Proteins are the molecular machines of living systems. Their dynamics are an intrinsic part of their evolutionary selection in carrying out their biological functions. Although the dynamics are more difficult to observe than a static, average structure, we are beginning to observe these dynamics and form sound mechanistic connections between structure, dynamics, and function. This progress is highlighted in case studies from myoglobin and adenylate kinase to the ribosome and molecular motors where these molecules are being probed with a multitude of techniques across many timescales. New approaches to time-resolved crystallography are allowing simple "movies" to be taken of proteins in action, and new methods of mapping the variations in cryo-electron microscopy are emerging to reveal a more complete description of life's machines. The results of these new methods are aided in their dissemination by continual improvements in curation and distribution by the Protein Data Bank and their partners around the world.

Keywords: Protein Data Bank; crystallography; electron microscopy; molecular dynamics; nuclear magnetic resonance (NMR); protein dynamics; structural biology; structure function.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Adenylate Kinase / chemistry*
  • Adenylate Kinase / genetics
  • Adenylate Kinase / metabolism
  • Animals
  • Databases, Protein*
  • Humans
  • Models, Molecular*
  • Myoglobin / chemistry*
  • Myoglobin / genetics
  • Myoglobin / metabolism
  • Ribosomes / chemistry*
  • Ribosomes / genetics
  • Ribosomes / metabolism
  • Structure-Activity Relationship

Substances

  • Myoglobin
  • Adenylate Kinase