Looking the interactions among amino acids in the attached file (hope the picture is clear enough), what will be the result of Asp-78 to Lys and His 48 to Lys mutations?
Hi Thanasis,
it depends on the gene and the species.
guessing it's in plants, you can select the genome if you see yours and test the prediction at http://sift.bii.a-star.edu.sg/sift4g/
or have a look at this paper: Article Developing maps of fitness consequences for plant genomes
hope this helps
fred
Getting rid of a histidine removes a "bend" in the primary structure of your amino acid sequence. Why are you changing the residues to lysine? Most folks would use an Alanine.
In biology, a mutation is the permanent alteration of the nucleotide sequence of the genome of an organism, virus, or extrachromosomal DNA or other genetic elements.
Mutations result from errors during DNA replication (especially during meiosis) or other types of damage to DNA (such as may be caused by exposure to radiation or carcinogens), which then may undergo error-prone repair (especially [microhomology-mediated end joining or cause an error during other forms of repair, or else may cause an error during replication (translesion synthesis). Mutations may also result from insertion or deletion of segments of DNA due to mobile genetic elements. Mutations may or may not produce discernible changes in the observable characteristics (phenotype) of an organism. Mutations play a part in both normal and abnormal biological processes including: evolution, cancer, and the development of the immune system, including junctional diversity.
regards
Thank you all for your answers! @ Katie A Burnette it is only a theoritical question for an enzymology course not something so special, but in your opinion will this affect the stability of this enzyme ? I think that's what this question wants to test. Just because Lys would not be the ideal residue (I know that too) what may it cause ?
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