This paper proposes a stock dynamic sizing optimization under the Logistic 4.0 environment. The safety stock is conceived to fill up the demand variability, providing continuous stock availability. Logistic 4.0 and the smart factory topics are considered. It focuses on vertical integration to implement flexible and reconfigurable smart production systems using the information system integration in order to optimize material flow in a 4.0 full-service approach. The proposed methodology aims to reduce the occurring stock-out events through a link among the wear-out items rate and the downstream logistic demand. The failure rate items trend is obtained through life-cycle state detection by a curve fitting technique. Therefore, the optimal safety stock size is calculated and then validated by an auto-tuning iterative modified algorithm. In this study, the reorder time has been optimized. The case study refers to the material management of a very high-speed train.
A computer program allowing post-translational modification sites assignment in proteins has been developed. The program has been constructed to elaborate data obtained from fast atom bombardment mass spectrometric mapping of polypeptides. The mass values of peptide(s) which cannot be assigned into the protein primary structure are elaborated by the program, which allows identification of the modified peptide(s) as well as the nature of the modifying group(s). This procedure has been applied to different kinds of post-translational events using three proteins as a model
In Northern Italy the coronavirus infection has spread since February 2020: the increase in admissions of COVID-19 patients corresponded to a drastic decrease in admissions of regular patients to the Emergency Room (ER). This retrospective study was conducted by Academy of Emergency Medicine and Care (AcEMC). During the lockdown period the accesses were reduced by more than 50%, and in the following months of May and June 2020, there was a recovery clearly below (70%) previous year’s numbers. We have observed a drastic reduction in white and green codes, a fair reduction in yellow codes, while red codes remained stable. The decrease in access to the ER mainly concerned patients with low priority color codes, but also the reduction in the number of accesses of yellow and red codes, insignificant at a superficial glance, is notable. If we consider that yellow and red codes during the months of the lockdown included many patients with COVIDrelated respiratory insufficiency, it is evident that there was a clear reduction in the number of serious illnesses not COVID-related. This is certainly another serious consequence of the COVID-19 pandemic.
We designed a computer program for the assignment of protein disulphides using mass spectrometric data. All the theoretical linear peptides containing from one to three cysteines are generated on the basis of the protein sequence. Their combination ways are determined in order to create all the possible disulphide-bridged fragments containing from two to six cysteines and to calculate their molecular weight. One, two and three S-S bridges per linked fragment were considered, taking into account the possibility that the fragments contain unabridged residues. The mass data obtained from the spectral analysis of peptide mixtures of the digested protein are then associated to the fitting structures of disulphide-bridged peptides, giving rise to the primary output. This output can then be screened by using information on the specificity of the proteolytic agent(s) used and/or any further mass data provided by Edman degradation and/or carboxypeptidase treatment of the peptide mixtures. The need for such a computer aid is discussed and examples of application are given.Key words: Disulfide bridge; Protein structure; Computer method; Mass spectrometry and the number of fragments, a single mass signal can be associated to many clusters of bridged peptides, with the ambiguity remaining still unsolved even after one step of chemical and/or enzymatic degradation [13].This paper describes the design and application of a computer program analyzing the possible solutions and filtering the results on the basis of new data obtained after degradation and/or information on the specificity of the proteolytic agent(s). We also suggest that such a computer aid can be indispensable in many cases for the unambiguous assignment of disulphide bridges.
Materials and methodsThe mass data and experimental procedures of the two proteins used in the application examples have already been reported [13,15]. Programs were written using Microsoft QuickBASIC (version 1.00b) and implemented on an Apple Macintosh LC 475 computer. The operative system was System 7.1. The compiled applications are compatible with all Apple Macintosh computers.
Results and discussion
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