Survey
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Short and Sweet Documentation It is very easy to document your work and it need not be as difficult as you might have learned in other classes ;) . However, the documentation shown below is for scientific writing. It probably won’t fly in your English class . . . Below are a few paragraphs that I wrote for a paper published in the journal Biochemistry. Please note that the sources are numbered as they appear in the paper. NOT alphabetically or by year, but when you use them. They are then assigned a number. If you go back and reuse that source, it is identified by its number. NFPs are the major axonal cytoskeletal components of neurons and are essential for establishing the correct diameters of large myelinated motor and sensory axons (1-3). The NFP assembly is composed of three different polypeptide subunits in the adult neuron: NFL (low molecular mass), NFM (intermediate molecular mass), and NFH (high molecular mass) (4-7) with apparent molecular masses as measured by SDS-polyacrylamide gel electrophoresis (PAGE) of 70, 150, and 200 kDa, respectively. Each polypeptide subunit is organized into three domains: a variable amino-terminal head domain, a central highly conserved segmented -helical rod domain of approximately 310 amino acids, and a hypervariable C-terminal tail domain (8). NFPs primarily located in the axon are reported to be highly phosphorylated in vivo (9). Static as well as dynamic properties of NFPs, including their assembly, stability, plasticity, and transport, are regulated by phosphorylation/dephosphorylation through kinase and phosphatase activities (10,11). Phosphorylation in the N-terminal head domain has been shown to have a regulatory role in subunit assembly and disassembly. Phosphorylation in the carboxy-terminal domains, particularly in NFM and NFH, has been implicated in the maintenance of axonal caliber (12,13), in determining the rate of transport of neurofilaments in the axon (14), in the promotion of cross-linking between the filaments, and in the maintenance of interactions with other cytoskeletal proteins (15). Various approaches have been used to evaluate the extent and sites of NFP phosphorylation in vivo. Proteolytic digestion of proteins followed by mass spectral analysis using HPLC-MS/MS and database searching have become popular for characterizing posttranslational phosphorylation (16). Phosphorylated sites of human NFH have been characterized by this method (9, 17). Some notes: Notice that almost all sentences are referenced!! You are writing a paper (this is an introduction) and giving lots of information that is NOT your own. Therefore every sentence should be attached to some reference. If multiple sentences in a row come from the same source you can reference at the end of the last sentence – however, you should not be predominantly relying on ONE source and then sprinkle your others throughout. All three sources should carry the load of the paper evenly!!! You may use the rule that many English instructors use when referencing: err on the side of caution – it is better to over-reference than it is to under-reference! Also, you can combine multiple sources into the same sentence!! Note above several instances where a sentence contains either two references (e.g. 10 and 11) or even portions of sentences are referenced to indicate which material came from which source (e.g. 12, 13, 14, and 15). Your bibliography would then number the references by how they appeared in the article. At this point in time, STYLE is not important. There is MLA, ACS, and other types of styles that are acceptable. For example, here are the first few references. These references are for journal articles that were used to write the above paragraphs. 1. Friede, R.L., and Samorajaski, T (1970) Anat. Rec. 167, 379-388. 2. Hoffman, P. N., Cleveland, D. W., Griffin, J. W., Landes, P.W. Cowan, N. J., and Price, D. L. (1987) Proc. Natl. Acad. Sci.. U.S.A. 84, 3472-3476. 3. Lee, M. K., and Cleveland, D. W., (1994) Curr. Opin. Cell Biol. 6, 34-40.