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Raw image files generated by fluorosequencing experiment represented in figure 4. The files are * Angiotensin_Norb_Alkyne.zip - This contains subfolderESN_2021_04_09_00_mx070 with nd2 files for 1 Pre, 3 Mocks and 10 Edman cycles. Sample results are represented as "blue" bars with legend Angiotensin-Alkyne * Angiotensin_negative.zip- This contains subfolderEN_2021_04_10_00_mx071 with nd2 files for1 Pre, 3 Mocks and 10 Edman cycles. Sample results are represented as "orange" bars with legend Angiotensin-Norbornenone * NegativeControl.zip - This contains subfolderESN_2021_04_11_00_jsp122 with nd2 files1 Pre, 3 Mocks and 10 Edman cycles. Sample results are represented as "gray" bars with legend Negative control peptide &nbsp

Hyaluronic acid (HA) is a linear high molecular weight glycosaminoglycan polymer with its molecular weight determining its physiological role, rheological properties and applications. The commercially used microbial source-Streptococcus zooepidemicus is incapable of synthesizing very high molecular weight polymer with low polydispersity, an essential niche in the HA market. In this organism, three important metabolic processes-glycolysis, hyaluronic acid synthesis and biomass formation compete for carbon source, nitrogen source, energy and precursors to determine the molecular weight of the synthesized polymer. After studying the role of culture conditions on these competing processes, it was found that the best strategy for enhancing molecular weight was to weaken the glycolytic process, strengthen HA synthesis process and maintain nitrogen under limiting condition to reduce the rate of biomass formation. Based on this newly developed strategy-temperature switches, addition of precursor N-acetylglucosamine and addition of pyruvate experiments enhanced the molecular weight of the polymer by 23%, 74% and 64%, respectively. Improving precursor levels, particularly UDP-N-acetylglucosamine and thereby strengthening the HA flux plays a direct role in improving molecular weight of hyaluronic acid. � 2009 Elsevier B.V. All rights reserved.

The software Peptide Fragment Ion Analyser (PFIA) aids in the analysis and interpretation of tandem mass spectrometric data of peptides. The software package has been designed to facilitate the analysis of product ions derived from acyclic and cyclic peptide natural products that possess unusual amino acid residues and are heavily post-translationally modified. The software consists of two programmes: (a) PFIA-I lists the amino acid compositions and their corresponding product ion types for 'a queried m/z value' (z = +1) and (b) PFIA-II displays fragmentation pattern diagram(s) and lists all sequence-specific product ion types for the protonated adduct of 'a queried sequence'. The unique feature of PFIA-II is its ability to handle cyclic peptides. The two programmes used in combination can prove helpful for deriving peak assignments in the de novo sequencing of novel peptides. Copyright � 2007 John Wiley & Sons, Ltd.