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Heat shock proteins are also believed to play a role in the presentation of pieces of proteins (or peptides) on the cell surface to help the immune system recognize diseased cells. [22] The major HSPs involved in the HSR include HSP70, HSP90, and HSP60. [5] Chaperones include the HSP70s and HSP90s while HSP60s are considered to be chaperonins. [17]
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]
Adjusting the human body temperature downward has been used therapeutically, in particular, as a method of stabilizing a body following trauma. It has been suggested that adjusting the adenosine A1 receptor of the hypothalamus may allow humans to enter a hibernation -like state of reduced body temperature, which could be useful for applications ...
Heat shock proteins (HSPs) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock , [ 1 ] but are now known to also be expressed during other stresses including exposure to cold, [ 2 ] UV light [ 3 ] and during wound healing or tissue remodeling. [ 4 ]
Elsewhere in the body, uncoupling protein activities are known to affect the temperature in micro-environments. [12] [13] This is believed to affect other proteins' activity in these regions, though work is still required to determine the true consequences of uncoupling-induced temperature gradients within cells. [12]
This results in the survival of the cell or organism, as if it were a wild type strain. In contrast, the nonpermissive temperature or restrictive temperature is the temperature at which the mutant phenotype is observed. Temperature sensitive mutations are usually missense mutations, which slightly modifies the energy landscape of the protein ...
Early research has suggested that cells which are better able to synthesize stress proteins and do so at the appropriate time are better able to withstand damage caused by ischemia and reperfusion. [15] In addition, many stress proteins overlap with immune proteins. These similarities have medical applications in terms of studying the structure ...
Temperature also modulates the activity of the Na + /K +-ATPase [citation needed]. The Na + /K +-ATPase is a P-type pump that extrudes 3Na + ions in exchange for 2K + ions for each hydrolytic cleavage of ATP. This results in a net movement of positive charge out of the cell, i.e. a hyperpolarizing current. The magnitude of this current is ...