Search results
Results from the WOW.Com Content Network
Among the tightest known protein–protein complexes is that between the enzyme angiogenin and ribonuclease inhibitor; the dissociation constant for the human proteins is 5x10 −16 mol/L. [3] [4] Another biological example is the binding protein streptavidin, which has extraordinarily high affinity for biotin (vitamin B7/H, dissociation ...
In biology, a pair bond is the strong affinity that develops in some species between a mating pair, often leading to the production and rearing of young and potentially a lifelong bond. Pair-bonding is a term coined in the 1940s [ 1 ] that is frequently used in sociobiology and evolutionary biology circles.
This glossary of biology terms is a list of definitions of fundamental terms and concepts used in biology, the study of life and of living organisms.It is intended as introductory material for novices; for more specific and technical definitions from sub-disciplines and related fields, see Glossary of cell biology, Glossary of genetics, Glossary of evolutionary biology, Glossary of ecology ...
In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin. In general, the interpretation of ligand is contextual with regards to what sort of binding has been observed.
Senescence (/ s ɪ ˈ n ɛ s ə n s /) or biological aging is the gradual deterioration of functional characteristics in living organisms. Whole organism senescence involves an increase in death rates or a decrease in fecundity with increasing age, at least in the later part of an organism's life cycle.
A chemical bond is the association of atoms or ions to form molecules, crystals, and other structures. The bond may result from the electrostatic force between oppositely charged ions as in ionic bonds or through the sharing of electrons as in covalent bonds, or some combination of these effects.
W (weak) and S (strong) are usually not swapped [15] but have been swapped in the past by some tools. [16] W and S denote "weak" and "strong", respectively, and indicate a number of the hydrogen bonds that a nucleotide uses to pair with its complementing partner. A partner uses the same number of the bonds to make a complementing pair. [17]
A unique intramolecular cysteine disulfide bonds in the ATP-binding domain of SrrAB TCs found in Staphylococcus aureus is a good example of disulfides in regulatory proteins, which the redox state of SrrB molecule is controlled by cysteine disulfide bonds, leading to the modification of SrrA activity including gene regulation.