Roderick MacKinnon determined three-dimensional molecular structure of potassium channel

Roderick MacKinnon – pioneer in ion channels in cell membranes

Article on Roderick MacKinnon

Biography & Contributions

Roderick MacKinnon is a professor of Molecular Neurobiology, Biophysics and Nobel laureate born on February 19, 1956. MacKinnon is received many notable awards and prizes like Newcomb Cleveland Prize in the year of 1997, W. Alden Spencer Award in the year of 1998, Rosenstiel Award in the year of 2000, Gairdner Foundation International Award in the year of 2001, Louisa Gross Horwitz Prize and Nobel Prize in Chemistry in the year of 2003.His works showed that short sequence of five amino acids acts to filter out sodium ions

The channel, MacKinnon discovered, has architecture sized in a way that easily strips potassium ions-but not sodium ions-of their associated water molecules and allows them to slip through. He also found a molecular “sensor” in the end of the channel nearest the cell’s interior that reacts to conditions around the cell, sending signals that open and close the channel at the appropriate times. MacKinnon and colleagues determined the three-dimensional molecular structure of a potassium channel from an actinobacteria, Streptomyces lividans, utilizing X-ray crystallography.

X-Ray crystallography

X-ray crystallography is a tool used for identifying the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions. X-ray crystallography is used to determine the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various materials, especially minerals and alloys. The method also revealed the structure and function of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystallography is still the chief method for characterizing the atomic structure of new materials and in discerning materials that appear similar by other experiments.

X-ray crystals structures can also account for unusual electronic or elastic properties of a material, shed light on chemical interactions and processes, or serve as the basis for designing pharmaceuticals against diseases. In a single-crystal X-ray diffraction measurement, a crystal is mounted on a goniometer. The goniometer is used to position the crystal at selected orientations. The crystal is bombarded with a finely focused monochromatic beam of X-rays, producing a diffraction pattern of regularly spaced spots known as reflections.

X-ray crystallography has led to a better understanding of chemical bonds and non-covalent interactions. The initial studies revealed the typical radii of atoms, and confirmed many theoretical models of chemical bonding, such as the tetrahedral bonding of carbon in the diamond structure, the octahedral bonding of metals observed in ammonium hexachloroplatinate (IV), and the resonance observed in the planar carbonate group and in aromatic molecules.

Integral Membrane Protein

Integral membrane protein is a type of membrane protein that is permanently attached to the biological membrane. It comprises a significant fraction of the proteins encoded in an organism's genome

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