For this purpose, the length of the intrinsically disordered Ser/Thr-rich 50-residue linker connecting a Clostridium thermocellum and a Clostridium cellulolyticum cohesin in a hybrid scaffoldin (Scaf4) was changed by sequences ranging from 4 to 128 residues.
Our results indicate that a propensity to form oligomers may be changed by local sequence variation in the Aβ linker region without mutating the charged residues.
These instructions can be changed by altering the sequence of the DNA that makes up the genes, which can account for many of the different characteristics found in humans and other animals.
The number of predicted TFs in each family may be changed by future updating of sequence versions and/or fine-tuning of gene annotations.
Enzyme function may be changed by intentionally altering the amino acid sequence (e.g., protein engineering).
This central dogma emphasises that our DNA sequence cannot be changed by our proteins, or by how they are changed by experience.
Summing up, the results of the present study suggest that the control of motor sequences can be changed by the interaction between giver and receiver: the interaction is characterized by a social affordance that the giver activates on the basis of social requests produced by the receiver.
Quasi-isotropic specimens increased in strength with size when the thickness was changed by repeating the sublaminate stacking sequence, with a 10% increase from a single to four stacked sublaminates.
Based on the intragenic variations, which are expected to contribute to the altered phenotype, we identified 139 proteins whose amino acid sequence is changed by SNVs, 28 proteins and 32 proteins which are affected by deletions and insertions respectively (Additional file 2 Table S2, Additional file 3: Table S3, Additional file 4: Table S4).
In order to proof this hypothesis by experimental data, the CUG, the AUG and both codon sequences together were changed by site directed mutagenesis creating three new expression constructs named PEG10-RF1a/2mutATG-His PEG10-RF1a/2mutATG-His PEG10-RF1a/2mutATG-HisG/CTG-His.
