protein conformations การใช้

• The closed and unoccupied state is the native protein conformation.
• The technology for studying protein conformation changes is really very poor compared to molecular biology,
• Modest changes in protein conformation and flexibility are also apparent in some of the catalytically impaired variants.
• Knowledge-based functions are formed with statistical models capturing aspects of the properties of native protein conformations.
• De novo programs will search three dimensional space and, in the process, produce candidate protein conformations.
• The denaturation of an egg is not a chemical reaction, but a change in the protein conformation.
• This approach operates under the assumption that local interactions play a large role in stabilizing the overall protein conformation.
• Ion channel mutations can alter protein conformation, and so change the amount of current flowing through these channels.
• Subdomains II and IV are cysteine-rich and most likely contribute to protein conformation and stability through the formation of disulfide bonds.
• Alternatively rotamer libraries of amino acid side chains that surround the binding cavity may be searched to generate alternate but energetically reasonable protein conformations.
• SNPs are alterations in the genetic code that can sometimes cause changes in protein conformation, as is the case with sickle cell anemia.
• 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.
• The protein has two binding sites for ATP  the active site is accessible in either protein conformation, but ATP binding to the inhibitor site stabilizes the conformation that binds F6P poorly.
• This model illustrates how the dynamics of phenomena such as alternate protein conformations, alternate oligomeric states, and transient protein-protein interactions can be harnessed for allosteric regulation of catalytic activity.
• Thus, in our 100 residue protein, and assuming that each amino acid has exactly 10 rotamers, a search algorithm that searches this space will have to search over 200 100 protein conformations.
• Whereas the shape complementarity based approaches are typically fast and robust, they cannot usually model the movements or dynamic changes in the ligand / protein conformations accurately, although recent developments allow these methods to investigate ligand flexibility.
• There is a transition state with a very specific transition volume, and by using supercritical carbon dioxide, you can return the egg to this transition volume and create a scenario in which the original protein conformation is favored.
• Although catalysis of the peptide bond involves the C2 hydroxyl of RNA's P-site adenosine in a proton shuttle mechanism, other steps in protein synthesis ( such as translocation ) are caused by changes in protein conformations.
• These energy functions typically simplify physical energy function and make them pairwise decomposable, meaning that the total energy of a protein conformation can be calculated by adding the pairwise energy between each atom pair, which makes them attractive for optimization algorithms.
• The resulting change in protein conformation could lead to phosphorylation of previously inaccessible phosphorylation sites on the C-terminus and the given phosphorylated segment could then liberate the transcription factor HY5 by competing for the same binding site at the negative regulator of photomorphogenesis COP1.