Related concepts (25)
Native state
In biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional. The native state of a biomolecule may possess all four levels of biomolecular structure, with the secondary through quaternary structure being formed from weak interactions along the covalently-bonded backbone. This is in contrast to the denatured state, in which these weak interactions are disrupted, leading to the loss of these forms of structure and retaining only the biomolecule's primary structure.
MilkyWay@home
MilkyWay@home is a volunteer computing project in the astrophysics category, running on the Berkeley Open Infrastructure for Network Computing (BOINC) platform. Using spare computing power from over 38,000 computers run by over 27,000 active volunteers , the MilkyWay@home project aims to generate accurate three-dimensional dynamic models of stellar streams in the immediate vicinity of the Milky Way. With SETI@home and Einstein@home, it is the third computing project of this type that has the investigation of phenomena in interstellar space as its primary purpose.
Roadrunner (supercomputer)
Roadrunner was a supercomputer built by IBM for the Los Alamos National Laboratory in New Mexico, USA. The US$100-million Roadrunner was designed for a peak performance of 1.7 petaflops. It achieved 1.026 petaflops on May 25, 2008, to become the world's first TOP500 LINPACK sustained 1.0 petaflops system. In November 2008, it reached a top performance of 1.456 petaFLOPS, retaining its top spot in the TOP500 list. It was also the fourth-most energy-efficient supercomputer in the world on the Supermicro Green500 list, with an operational rate of 444.
Binding site
In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins (resulting in a protein-protein interaction), enzyme substrates, second messengers, hormones, or allosteric modulators. The binding event is often, but not always, accompanied by a conformational change that alters the protein's function.
Protein aggregation
In molecular biology, protein aggregation is a phenomenon in which intrinsically-disordered or mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly. Protein aggregates have been implicated in a wide variety of diseases known as amyloidoses, including ALS, Alzheimer's, Parkinson's and prion disease. After synthesis, proteins typically fold into a particular three-dimensional conformation that is the most thermodynamically favorable: their native state.

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