Kurt Wüthrich

Kurt Wüthrich is a Swiss chemist who developed nuclear magnetic resonance methods for determining protein structures in solution. He received the 2002 Nobel Prize in Chemistry.

Nuclear magnetic resonance: A spectroscopic method that uses the magnetic properties of atomic nuclei to probe their chemical environments. Wüthrich adapted this method to determine protein structures in solution.
Sequential assignment: The process of matching NMR signals to successive residues along a protein's amino-acid chain. Wüthrich's approach used short-range connectivities to assign signals residue by residue.
Richard R. Ernst: A Swiss chemist whose work on Fourier-transform and multidimensional NMR earned the 1991 Nobel Prize in Chemistry. Ernst's NMR advances helped make Wüthrich's multidimensional protein studies possible.
Protein dynamics: The time-dependent motions and conformational changes of proteins at molecular scales. Solution NMR can probe motions that a single static protein model cannot show.
Protein Data Bank: An open archive of experimentally determined three-dimensional structures of biological macromolecules. NMR structures became a substantial part of the archive alongside crystallographic models.
Protein structure: The three-dimensional arrangement of atoms in a protein, including its folding and molecular interactions. This is the structural information his NMR methods were designed to reveal.
NOESY: A two-dimensional NMR experiment that detects cross-relaxation between nearby nuclear spins. NOESY cross-peaks provided the interatomic distance information used in structure determination.
Christian B. Anfinsen: An American biochemist who demonstrated that a protein's amino-acid sequence can determine its native structure. Anfinsen's folding principle framed the biological significance of Wüthrich's structural measurements.
Intrinsically disordered protein: A protein or protein region that lacks a single stable three-dimensional structure under physiological conditions. NMR methods developed for solution samples are suited to studying disordered regions.
NMR spectroscopy: A family of techniques that uses nuclear magnetic resonance to study molecular structure and dynamics. Wüthrich helped expand this broader toolkit into protein structural analysis.

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John B. FennRelated: Wüthrich received the same prize for a different contribution to studying biological macromolecules.