The phrase "affinity loss" is correct and usable in written English.
It can be used in contexts related to chemistry, biology, or psychology, where it refers to a decrease in attraction or connection between entities.
Example: "The study revealed a significant affinity loss between the two molecules under high temperature conditions."
Alternatives: "decrease in affinity" or "loss of attraction".
Both suffered their largest affinity loss when binding variant M1.
The binding profile is characterized using two metrics, the worst-fold affinity loss and the weakest binding affinity.
Two compounds remained potent against the panel with less than 15-fold affinity loss, and four had moderate shifts of less than 80-fold loss.
The worst-fold affinity loss is the ratio between the weakest binding affinity (Ki) of a compound for a protease variant and its affinity for wild-type protease.
(2) The binding specificity profiles of the new compounds fall into two classes: six that remained potent or had a moderate shift against the mutant panel (<50-fold affinity loss) and two that were more susceptible to resistance mutations (>80-fold affinity loss).
The dominant effect of the Rap1– Rifusionusinn in diploid cells and its ability to shorten telomeres in haploids may be due to altered cell cycle regulation, altered affinity, loss of end protection, or a combination of these factors.
The presence of DOTA at the N-terminus has caused minor affinity losses for all subtypes, which were more pronounced for sst1 and sst5.
Interestingly, AF-71 and AF-80, the two relatively weak binders to wild-type protease, had rather flat binding specificity profiles with worst-fold affinity losses of 13 and 11, respectively.
AF-71 and AF-80, involving the same R3 substitution with a double-ring aromatic system, had violation amounts of about 20 Å but worst-fold affinity losses of only about 10.
This is by no means a highly quantitative relationship; for example, compounds with larger envelope violations can have smaller worst-fold affinity losses (AF-78 vs AF-69), particularly against a relatively small panel of mutants.
Because WT ToMOH and mutants N202A and Q228A maintain a similar ToMOD-Fl binding affinity, the loss of coupling efficiency in these mutants cannot be attributed to a decreased binding affinity for the regulatory protein.
