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FLIP is often used and is closely associated with Fluorescence recovery after photobleaching (FRAP). The major difference between these two microscopy techniques is that FRAP involves the study of a cell’s ability to recover after a single photobleaching event whereas FLIP involves the study of how the loss of fluorescence spreads throughout ...
An open reading frame (ORF) is a reading frame that has the potential to be transcribed into RNA and translated into protein. It requires a continuous sequence of DNA which may include a start codon, through a subsequent region which has a length that is a multiple of 3 nucleotides, to a stop codon in the same reading frame.
The frame problem occurs even in very simple domains. A scenario with a door, which can be open or closed, and a light, which can be on or off, is statically represented by two propositions and .
This project is inspired by the 2009 Wikipedia AP Biology Project. There are many basic and important diagrams missing from biological articles and we're doing our part to fix this. Students will work alone, there are 23 students so we should have 23 new images with captions and labels. The time frame will be three weeks.
This figure depicts how Floxing is used in scientific research for spatial and temporal control of gene expression. In genetic engineering, floxing refers to the insertion of a DNA sequence (which is then said to be floxed) between two LoxP sequences, creating an artificial gene cassette which can then be conditionally deleted (knocked out), translocated, or inverted in a process called Cre ...
The split gene theory is a theory of the origin of introns, long non-coding sequences in eukaryotic genes between the exons. [1] [2] [3] The theory holds that the randomness of primordial DNA sequences would only permit small (< 600bp) open reading frames (ORFs), and that important intron structures and regulatory sequences are derived from stop codons.
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
The scar site causes a frame shift which prevents the continuous reading of codons, which is required for the formation of fusion protein. Tom Knight later developed the BB-2 assembly standard in 2008 to address problems with joining the scars of protein domains and that the scars consist of eight bases, which will yield an altered reading ...