The evolution of protein NMR

2013/11/01 by Iain D. Campbell · 8 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Mathematics · #Lipid Membrane Structure and Behavior #Supramolecular Chemistry and Complexes #Advanced NMR Techniques and Applications #Nanotechnology #Focus (optics) #Domain (mathematical analysis) #Data science #Computational biology #Computer science #Chemistry #Biology #Physics #Materials science #Mathematics

paper · pdf · doi:10.3233/bsi-130055

published in Biomedical Spectroscopy and Imaging 2(4), 245-264 (IOS Press)

openalex publication_date 2013/11/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/05/21

Abstract

Since the first NMR spectrum of a protein was published over 50 years ago, remarkable technical improvements have led to NMR being recognized as a uniquely powerful tool that can give a wide variety of useful information about macromolecules and their interactions. This article gives an overview of NMR studies of proteins. It presents a personal historical perspective, briefly reviews the current status of the field and reflects on possible future directions. Two specific examples, related to multi-domain complexes and membrane-spanning adhesion receptors, are described to illustrate recent applications. Emphasis is placed on how general advances in molecular biology and technology are changing the nature and focus of NMR studies.

Citations

• A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis
• Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
• The final steps of integrin activation: the end game
• Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networks

Cited by

• Structural biology [wikipedia]