Structural biology

Structural biology studies the three-dimensional structures of biological molecules and how those structures relate to their functions.

X-ray crystallography: A method that determines atomic structures by analyzing how crystals diffract X-rays. It established atomic-resolution structure determination for many proteins and other biomolecules.
Protein structure: The three-dimensional arrangement of atoms in a protein, from local patterns to its overall fold. Protein structures are a central target of structural biology.
Structure-based drug design: Drug discovery that uses a target molecule’s three-dimensional structure to guide compound design. Atomic models can identify binding pockets and suggest modifications to candidate drugs.
Max Perutz: A British molecular biologist who pioneered protein crystallography and determined hemoglobin’s structure. His crystallographic work helped establish structural biology as an experimental discipline.
Intrinsically disordered protein: A protein or protein region that lacks a single stable three-dimensional structure under physiological conditions. Structural methods must account for ensembles rather than one fixed molecular model.
Cryo-electron microscopy: A method that images rapidly frozen specimens with an electron microscope to reconstruct molecular structures. It reveals structures of large complexes without requiring them to form crystals.
Nucleic acid structure: The three-dimensional organization of DNA and RNA molecules and their interactions. DNA and RNA structures explain recognition, regulation, and molecular function.
Enzyme mechanism: The sequence of molecular events by which an enzyme catalyzes a chemical reaction. Active-site structures help explain how enzymes bind substrates and catalyze reactions.
John Kendrew: A British biochemist who determined the first atomic-resolution protein structure, that of myoglobin. His myoglobin structure demonstrated that a protein’s atomic arrangement could be solved.
Protein conformational ensemble: The set of structural states a protein occupies and interconverts among under specified conditions. A single structure often cannot capture functionally relevant molecular motion.

Linked from 12 pages