The paths to the atomic structures of proteins and nucleic acids

Abstract

AbstractAtomic structures of large biological molecules were first established by scattering X-rays in protein crystals and later with crystals of nucleic acids. Good crystals allow for an accuracy of 0.1 Å (10−11 m) that may reveal details of catalytic processes. The novel cryo-electron microscopy method does not need crystals and it can establish chain folds confidently. Chain folds can also be derived from NMR data to produce numerous binary atomic distances. Recently, chain folds for a given amino acid sequence were derived by mere computing, based on the presently available large library of proteins that are related by their amino acid sequences and structures. Graphical abstract