α is the multiplicative factor by which a mutator mutation increases the somatic mutation rate per cell generation, e.g. the magnitude of the genetic instability.
In Lmb, RIP mutation increases the speed with which the detrimental genes can be mutated to extinction, rendering migration of low importance compared to the ability to generate variants locally in a single sexual cycle.
The E22Q mutation increases the population with intact VGSN turn compared to the wild-type (WT) peptide.
Follow-up studies should clarify whether the Glu318Gly mutation increases the risk of cognitive decline in later life.
pH versus kcat profiles show that this mutation increases the acidity of the catalytic general acid Tyr55.
The E37A mutation increases the affinity of TetR for tetO variants and seems to be essential for binding to modified operator sequences.
In addition to the conformational changes described above, we hypothesized that the G118V mutation increases the local hydrophobicity of the polypeptide, the structural consequences of which would be amplified by the presence of another valine residue at position 119.
Nevertheless, it appears that factor V Leiden or G20210A prothrombin gene mutation increases the risk of venous thromboembolism about 2- to 4-fold, compared with patients with cancer without either of these mutations.
The K28A mutation increases the intrapeptide hydrophobic interactions that promote population of structures in Basin I and Basin II whose structures are characterized by hydrophobic interaction between V24 and K28 side chains but with well-separated ends of the backbone atoms in the VGSN turn.
From NMR lineshape analysis, we find the G29A mutation increases the folding rate constant by threefold; the folding time is 3 microsec.
These results indicate that the Ghd10 mutation increases the plant height, panicle length and primary branch number in addition to delaying the heading date.
