mCherry is a red fluorescent protein (RFP), classified as a luminescent protein, that belongs to a group of fluorescent protein chromophores. mCherry is a part of the mFruits protein family, which is a family of mRFPs, monomeric red fluorescent proteins. mCherry’s amino acid sequence positions it taxonomically in the green fluorescent protein, GFP, superfamily of proteins; these proteins all have fluorescent and bioluminescent functions and includes proteins such as DsRed, GFP, mStrawberry, and mOrange. Specifically, mCherry is known as being derived from the protein DsRed, which was originally found in Discosoma species, most often Discosoma sea anemones.

Wu, B., Chen, Y., & Müller, J. D. (2009). Fluorescence fluctuation spectroscopy of mCherry in living cells. Biophysical journal, 96(6), 2391–2404. https://doi.org/10.1016/j.bpj.2008.12.3902

mCherry is visible under UV light, making it a photoprotein, which aids in its ease of detection. mCherry emits light between 550 and 650 nm and absorbs light between 540 and 590 nm and uses pi-electron conjugation to produce a red emission and absorption. The quantum yield, as explained by the non-planarity of the chromophore, which, in mCherry, is extended, is 0.22. mCherry is constitutively fluorescent, meaning it can be visible, in at least some degree, at any time by use of the UV spectra. mCherry is most often visualized via fluorescence spectroscopy or fluorescence microscopy. This protein exists in multiple brightness states, which means that mCherry’s visual emission fluctuates in amplitude. These states are useful since their brightness is not dark, like it is with mCherry’s relative, the fluorescent protein mRFP1, but instead has long-lived, two states with differing values in brightness, which include bright and dim states.

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Shu, X., Shaner, N. C., Yarbrough, C. A., Tsien, R. Y., & Remington, S. J. (2006). Novel chromophores and buried charges control color in mFruits. Biochemistry, 45(32), 9639–9647. https://doi.org/10.1021/bi060773l

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Route15Maryland

Shu, X., Shaner, N. C., Yarbrough, C. A., Tsien, R. Y., & Remington, S. J. (n.d.). 2H5Q: Crystal structure Of mcherry. Retrieved March 28, 2021, from https://www.ncbi.nlm.nih.gov/Structure/pdb/2H5Q

Miyawaki, A., Shcherbakova, D. M., & Verkhusha, V. V. (2012). Red fluorescent proteins: chromophore formation and cellular applications. Current opinion in structural biology, 22(5), 679–688. https://doi.org/10.1016/j.sbi.2012.09.002

The functional domains seen in both alpha helices and beta sheets present in the mCherry protein are related to those found in GFP-like, or fluorescent, proteins. Thus, the folds that these domains undertake are common in most GFP-like proteins, especially those that have a fluorescent or luminescent function. Likewise, the domains present only in the beta barrel portion of the protein are also homologous to the domains found in GFP and GFP-related proteins, such as mStrawberry and mOrange. These proteins contain a similar structure to mCherry, which means they also contain a beta barrel that composes most of their three-dimensional structure with the same domains that are present in mCherry’s beta barrel. The beta barrel of mCherry, since it is closely related to the beta barrel of other mFruits, and is a derivative of DsRed, contains a weakness between beta sheet 7 and beta sheet 10, as is seen with all other mFruit beta barrels, originating in the DsRed fluorescent protein. This weakness stems from parental DsRed being a tetrameric protein and causes an increase in permeability to oxygen.

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Route15NJ closed

US 15 continues as a freeway until it intersects U.S. Route 11 and Pennsylvania Route 581 in Camp Hill. US 15 runs concurrent with US 11, passing Harrisburg on the west shore of the Susquehanna River. The concurrency ends at Shamokin Dam, where US 11 splits and follows the North Branch Susquehanna River, and US 15 follows the West Branch Susquehanna River north towards Williamsport where it passes through Lewisburg and the campus of Bucknell University (which is partially bisected by the highway). In the future, US 15 and US 11 will diverge in Selinsgrove, Pennsylvania, from which US 15 will proceed north on a road yet to be built, and connect back to its current alignment near Winfield, PA. 11 will be joined to a business loop of 15 instead of the main route.

US 15 starts in Maryland at Point of Rocks, crossing the Potomac River and then merges into US 340 just south of Frederick. In Frederick, US 40 merges with US 15 for a very short distance. From there US 15 goes through Thurmont and on to the Maryland/Pennsylvania border.

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The segment from Williamsport, Pennsylvania to the northern terminus at I-86 and NY 17 in Painted Post, New York has been completely upgraded to Interstate standards in preparation for the eventual transition to designation as I-99, as has the US 15/I-86 interchange. The 12.59-mile (20.26 km) segment of US 15 in New York runs parallel to the Tioga River from the state line to its current northern terminus at I-86 and NY 17 exit 44 at the junction of the Tioga and Cohocton rivers in Painted Post, west of downtown Corning. The entire length of US 15 in New York is signed concurrently with I-99.

As mentioned above, the ligand for mCherry is the CH6, which is a popular chromophore among red fluorescent proteins. This molecule, which is characterized as a methionine, tyrosine, and glycine chromophore, has a formula of C16H19N3O4S, with a molecular weight of 349.9 grams/mol, and is the molecule responsible for giving mCherry its red color and fluorescent properties. The CH6 chromophore is similar to the ligand of DsRed and related mFruit fluorescent proteins; the relationship is known by the similarities in the extension of the pi-system of GFP’s chromophore, specifically the extension of another N-acylimine group, between the chromophore present in mCherry and the parental DsRed. The chromophore binds to mCherry via L-peptide linkages and is structurally supported by noncovalent interactions within the central helix. Two alpha helices in the central helix core are bound to the chromophore via L-peptide linkages, producing two of the alpha helices with the chromophore in between them all within the beta barrel. Serine69 on one alpha helix forms a peptide linkage with the chromophore at a carboxyl carbon. This same carboxyl carbon forms another peptide linkage with the second alpha helix on the amino acid residue phenylalanine65. Due to these binding locations and residues, in mCherry, the imidazoline ring and the phenolate rings of the CH6 chromophore, when bound to the polypeptide in its fully folded three-dimensional structure, have tilt and twist angles of 11 and 14 degrees, respectively.

US 15 enters Pennsylvania south of Gettysburg. Business Route 15 (Emmitsburg Road) goes through Gettysburg, while US 15 bypasses the borough; the bypass continues to York Springs. US 15 passes through Dillsburg before becoming a freeway near Grantham and the Messiah College campus.

Route15nj map

The official biological process of mCherry is bioluminescence and this process allows mCherry to aid in the generation of precursor metabolites and gene expression analytics. mCherry is most commonly used as a fluorescent reporter, acting as a labeled tag for genes, cells, or organelles of interest. The emissive and fluorescent properties allow this protein to function as an intracellular probe, used especially for viewing constitutive gene expression. mCherry is a very valuable protein due to its function as a fluorescent tag, allowing different cell components to be viewed in a variety of scenarios, such as analyzing gene expression, genome editing, and identifying species of microorganisms. mCherry is also used for protein study and research, as it is a common spectroscopic label that can identify the mobility, localization, and interactions of different proteins in tissues, cells, and organelles. mCherry, along with being used to analyze gene expression, is also commonly used to analyze the specific functions of these genes within the cell. mCherry is used for long-term studies, both in vivo and in vitro, since it has high photostability, which makes it a very common protein to use, especially in the fields of biotechnology. Also, mCherry is among one of the most popular mFruit proteins used for cell biology research due to its high photostability, maturation properties, and tagging tolerance.

Route15Map

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US 15-401 continues to Laurinburg, at which US 401 splits off and US 15 runs concurrent with US 501. US 1 briefly merges with US 15-501 through Aberdeen and Sanford. The route continues north of Sanford with NC 87 towards Pittsboro. Past Pittsboro, US 15-501 goes toward Chapel Hill and skirts around the southeastern edge of the city and then across I-40 to Durham. (Prior to the construction of the Chapel Hill bypass, US 15 ran through Chapel Hill, and as of 2018 there is a "Jefferson Davis Highway" marker on Franklin Street, Chapel Hill's main street.[2]) Here US 15-501 splits into Business and Bypass routes. Before US 15 Business and Bypass highways rejoin on the other side of Durham, I-85 merges into US 15 Business. Then I-85/US 15 go north. Right after crossing Falls Lake at exit 186, US 15 splits off to the east. US 15 runs parallel to I-85, going through the city of Creedmoor. It then crosses back over I-85, goes through the city of Oxford, on through Bullock, and then to the N.C.-Virginia state line.

US 15 Route information Existed 1926-present Location Country United States States South Carolina, North Carolina, Virginia, Maryland, Pennsylvania, New York U.S. Route 15 (US 15) is a 791.71 mi (1,274.13 km)-long United States highway, designated along South Carolina, North Carolina, Virginia, Maryland, Pennsylvania, and New York. The route is signed north–south, from U.S. Route 17 Alternate in Walterboro, South Carolina to NY 17 in Corning, New York. It is one of the original United States Highways from 1926.

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U.S. Route15

Karimi, S., Ahl, D., Vågesjö, E., Holm, L., Phillipson, M., Jonsson, H., & Roos, S. (2016). In Vivo and In Vitro Detection of Luminescent and Fluorescent Lactobacillus reuteri and Application of Red Fluorescent mCherry for Assessing Plasmid Persistence. PloS one, 11(3), e0151969. https://doi.org/10.1371/journal.pone.015196

Subach, F. V., Patterson, G. H., Manley, S., Gillette, J. M., Lippincott-Schwartz, J., & Verkhusha, V. V. (2009). Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nature methods, 6(2), 153–159. https://doi.org/10.1038/nmeth.1298

Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N., Palmer, A. E., & Tsien, R. Y. (2004). Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nature biotechnology, 22(12), 1567–1572. https://doi.org/10.1038/nbt1037

Rt 15NJ

Virginia's section of US 15 starts in Mecklenburg County. Not far from the state line, it crosses a narrow finger of the John H. Kerr Reservoir. The highway goes through the town of Clarksville and merges very briefly with US 58/VA 49 and then crosses over the main body of Lake Kerr. US 15 continues a little ways and merges with US 360. The two highways go on to the town of Keysville. After Keysville, US 15 branches off and goes to the town of Farmville. After a brief merge with US 460, US 15 goes through the towns of Dillwyn, New Canton (on the James River), Fork Union, and Palmyra before crossing I-64 at Zion Crossroads. After passing the interstate, US 15 goes through the towns of Gordonsville (with a quick merge with US 33) and Orange, and then on to Culpeper. After Culpeper US 15 runs concurrent with US 29. In Warrenton they briefly merge with US 17. South of Gainesville US 15 breaks off and crosses I-66. From there it goes on to Leesburg and then to the state line.

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The gene responsible for mCherry is 711 base pairs and is oftentimes inserted and transcribed from plasmids to obtain a sizable quantity for the tagging and probing of cellular components. mCherry is a protein that contains 236 amino acids and has a mass of 26.7 kDa, making it a low molecular weight protein that often folds faster than tetrameric proteins, such as its parent DsRed. The amino acids with the highest count in the mCherry primary sequence are lysine, glycine, and glutamate, each of which are in mCherry’s primary structure 24 times, each composing 10% of the entire sequence. The amino acid with the least number of residues in the primary sequence of mCherry is alanine, with only 11 residues, making up only 5% of the protein’s sequence. The total atom count in mCherry is 2121 and the whole protein is composed of only one peptide chain, thus leading to a tertiary structure once fully folded. The complete three-dimensional structure of mCherry has been determined by x-ray diffraction which gave an experimental resolution of 1.36 angstroms. mCherry is composed of only three alpha helices with a that is made up of 13 beta sheets. Thus, the protein is composed mostly of beta sheets which surround the chromophore (ligand) and as a barrel-like structure, which shields the chromophore and central helix from the cytosolic environment.

Route15NJ accident today

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Starting at ALT US 17 in Walterboro US 15 goes east. It runs parallel to I-95 and across I-26. Then it turns north and crosses I-95. Just before the town of Santee US 15 converges with US 301. In Santee the two highways merge with I-95 at exit 98 and all three cross Lake Marion. At exit 102, US 15/301 split off from I-95 and go into the town of Summerton. US 15 then separates from US 301 and heads mainly north to city of Sumter. From there it continues north, crosses I-20, goes through the cities of Bishopville and Hartsville to the town of Society Hill. It is here that US 401 joins US 15 and both go to the North Carolina border.

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Laurent, A. D., Mironov, V. A., Chapagain, P. P., Nemukhin, A. V., & Krylov, A. I. (2012). Exploring structural and optical properties of fluorescent proteins by squeezing: modeling high-pressure effects on the mStrawberry and mCherry red fluorescent proteins. The journal of physical chemistry. B, 116(41), 12426–12440. https://doi.org/10.1021/jp3060944

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The chromophore-binding domain, the functional area of mCherry that is responsible for binding the chromophore that gives it its color, is due mainly to 3 residues – tyrosine72, glycine73, and methionine71. Once mCherry is translated in the cell on a ribosome, these chromophore-binding amino acids are modified with imidazoline groups via post-translational modification. The red emission is produced by the generation of an acylimine linkage in the backbone of the polypeptide during a second oxidation step that occurs due to illumination with UV light. The chromophore environment is then indirectly modified to produce the red emission shift that can be seen with fluorescence spectroscopy or microscopy. This indirect modification includes the movement of the charged lysine70 residue and the protonation of the glutamine215 residue, both of which alter the distribution of the electron-density in the chromophore, thus causing the red emission.