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Protein side chains exhibit rotamers, whose distribution is determined by their steric interaction with different conformations of the backbone. This effect is evident from statistical analysis of the conformations of protein side chains in the Backbone-dependent rotamer library .
A protein fold refers to the general protein architecture, like a helix bundle, β-barrel, Rossmann fold or different "folds" provided in the Structural Classification of Proteins database. [11] A related concept is protein topology.
Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organization of the protein backbone in 3D and serves as a visual framework for hanging details of the entire atomic structure ...
A change in protein conformation produces a change in the net orientation of the dye relative to the surface plane and therefore the intensity of the second harmonic beam. In a protein sample with a well-defined orientation, the tilt angle of the probe can be quantitatively determined, in real space and real time.
A network of alternative conformations in catalase (Protein Data Bank code: 1gwe) with diverse properties. Multiple phenomena define the network: van der Waals interactions (blue dots and line segments) between sidechains, a hydrogen bond (dotted green line) through a partial-occupancy water (brown), coupling through the locally mobile backbone (black), and perhaps electrostatic forces between ...
A protein folded into its native state or native conformation typically has a lower Gibbs free energy (a combination of enthalpy and entropy) than the unfolded conformation.A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment.
This protein was the first to have its structure solved by X-ray crystallography by Max Perutz and John Kendrew in 1958, for which they received a Nobel Prize in Chemistry A biomolecule or biological molecule is loosely defined as a molecule produced by a living organism and essential to one or more typically biological processes . [ 1 ]
The sequential model (also known as the KNF model) is a theory that describes cooperativity of protein subunits. [1] It postulates that a protein's conformation changes with each binding of a ligand, thus sequentially changing its affinity for the ligand at neighboring binding sites.