protein | Protein subunit | Protein-protein interaction | Hfq protein | protein domain | Protein-protein_interaction | Protein Data Bank | RNA-binding protein | Promyelocytic leukemia protein | G protein | Wiskott–Aldrich syndrome protein | Protein G | protein dimer | Protein A | C-reactive protein | Bone morphogenetic protein 2 | AMP-activated protein kinase | Transmembrane protein | Tau protein | Sterol regulatory element-binding protein | SR protein | Rab escort protein | Protein structure | protein structure | Protein phosphatase 2 | protein kinase | Protein Information Resource | Protein folding | protein folding | Protein domain |
Researchers such as Francisco Blanco et al. have used protein NMR to show that beta-hairpins can be formed from isolated short peptides in aqueous solution, suggesting that hairpins could form nucleation sites for protein folding.
These have been uploaded by researchers who have characterized the structure of molecules usually by X-ray crystallography, NMR spectroscopy or electron microscopy.
Membrane proteins and amyloid fibrils, the latter related to Alzheimer's disease and Parkinson's disease, are two examples of application where solid-state NMR spectroscopy complements solution-state NMR spectroscopy and beam diffraction methods (e.g. X-ray crystallography, electron microscopy).