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发布于:2023-3-23 09:44:57  访问:71 次 回复:0 篇
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Covery price by randomly permuting the information 1,000 instances and comparing the
Approximately 80 of identified proteins are within 1 common Title Loaded From File deviation of the mean alter in abundance. Bottom: the top 15 most abundant proteins have been identified and are, from left to ideal, eukaryotic translation elongation issue 1 three (Cre06.g263450), eukaryotic translation elongation issue 1 two (132905), ribulose-1,5-bisphosphate carboxylase/oxygenase massive subunit (41179049), isocitrate lyase (Cre06.g282800), fructose-1,6-bisphosphate aldolase (Cre05.g234550), S-adenosyl homocysteine hydrolase (Cre03.g204250), cobalamin-independent methionine synthase (Cre03.g180750), 2-cys peroxiredoxin (Cre06.g257601), glyceraldehyde-3phosphate dehydrogenase (Cre01.g010900), enolase (Cre12.g513200), pre-apoplastocyanin (Cre03.g182551), ribulose-1,5-bisphosphate carboxylase/oxygenase smaller subunit (108283), oxygen-evolving enhancer protein 2 (Cre12.g550850), phosphoenolpyruvate carboxykinase (Cre02.g141400), and unnamed protein (Cre12.g528000). B, representative plot on the ratio of protein abundance among copper-deficient and copper-replete cells. Roughly 20 with the information lie outdoors 1 common deviation, and only 5 of information lie outside 2 common deviations.Covery rate by randomly permuting the data 1,000 occasions and comparing the amount of changes observed within the permutated runs to the quantity of alterations inside the genuine experiment. Making use of this method, we estimated a 20 false discovery rate in figuring out when a adjust in abundance occurred for our information. Using TMHMM, we examined the prevalence of transmembrane domains in our proteomics dataset. The TMHMM technique, when tested on a set of 645 proteins with known three-dimensional structures, was able to accurately discriminate in between soluble and membrane proteins with an accuracy of 99 (45). In our dataset, involving five and 6 of all proteins in each and every study have been located to contain a minimum of a singleMolecular Cellular Proteomics 12.The Proteome of Micronutrient Deficiency in Chlamydomonas reinhardtiiFIG. 3. Statistical overview of reproducibility from the proteomics dataset. A, prime: representative log10 ratio of protein abundance of metal-deficient cells versus metal-replete cells. About 80 of identified proteins are inside 1 normal deviation of the mean modify in abundance.Covery price by randomly permuting the information 1,000 times and comparing the amount of alterations observed in the permutated runs for the variety of alterations in the true experiment. Making use of this approach, we estimated a 20 false discovery rate in figuring out when a change in abundance occurred for our information. Working with TMHMM, we examined the prevalence of transmembrane domains in our proteomics dataset. The TMHMM method, when tested on a set of 645 proteins with known three-dimensional structures, was capable to accurately discriminate involving soluble and membrane proteins with an accuracy of 99 (45). In our dataset, amongst five and 6 of all proteins in every study had been found to include at least a singleMolecular Cellular Proteomics 12.The Proteome of Micronutrient Deficiency in Chlamydomonas reinhardtiiFIG. three. Statistical overview of reproducibility of your proteomics dataset. A, leading: representative log10 ratio of protein abundance of metal-deficient cells versus metal-replete cells. About 80 of identified proteins are inside 1 common deviation of the mean modify in abundance. Bottom: the leading 15 most abundant proteins had been identified and are, from left to appropriate, eukaryotic translation elongation aspect 1 three (Cre06.g263450), eukaryotic translation elongation factor 1 2 (132905), ribulose-1,5-bisphosphate carboxylase/oxygenase huge subunit (41179049), isocitrate lyase (Cre06.g282800), fructose-1,6-bisphosphate aldolase (Cre05.g234550), S-adenosyl homocysteine hydrolase (Cre03.g204250), cobalamin-independent methionine synthase (Cre03.g180750), 2-cys peroxiredoxin (Cre06.g257601), glyceraldehyde-3phosphate dehydrogenase (Cre01.g010900), enolase (Cre12.g513200), pre-apoplastocyanin (Cre03.g182551), ribulose-1,5-bisphosphate carboxylase/oxygenase tiny subunit (108283), oxygen-evolving enhancer protein two (Cre12.g550850), phosphoenolpyruvate carboxykinase (Cre02.g141400), and unnamed protein (Cre12.g528000).
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