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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation, radiation, or heat. [3]
RuBisCO is important biologically because it catalyzes the primary chemical reaction by which inorganic carbon enters the biosphere.While many autotrophic bacteria and archaea fix carbon via the reductive acetyl CoA pathway, the 3-hydroxypropionate cycle, or the reverse Krebs cycle, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO.
At high temperatures, these interactions cannot form, and a functional protein is denatured. [25] However, it relies on two factors; the type of protein used and the amount of heat applied. The amount of heat applied determines whether this change in protein is permanent or if it can be transformed back to its original form. [26]
The cyclic light-dependent reactions occur only when the sole photosystem being used is photosystem I. Photosystem I excites electrons which then cycle from the transport protein, ferredoxin (Fd), to the cytochrome complex, b 6 f, to another transport protein, plastocyanin (Pc), and back to photosystem I. A proton gradient is created across the ...
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
These conformational changes, as a result of protein adsorption, can also denature the protein and change its native properties. Illustration of protein (green) ligand (red star) binding site alteration by the conformational change of the protein as a result of surface (blue) adsorption. Note how the ligand no longer fits into the binding site.
This happens when light is available, as the ferredoxin protein is reduced in the photosystem I complex of the thylakoid electron chain when electrons are circulating through it. [13] Ferredoxin then binds to and reduces the thioredoxin protein, which activates the cycle enzymes by severing a cystine bond found in all these enzymes. This is a ...
Cyanobacteria photosystem II, dimer, PDB 2AXT. Photoinhibition occurs in all organisms capable of oxygenic photosynthesis, from vascular plants to cyanobacteria. [14] [15] In both plants and cyanobacteria, blue light causes photoinhibition more efficiently than other wavelengths of visible light, and all wavelengths of ultraviolet light are more efficient than wavelengths of visible light. [14]