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https://www.selleckchem.com/btk.html Many classes of key functional proteins such as transcription factors or cell cycle proteins are present in the proteome at a very low concentration. These low-abundance proteins are almost entirely invisible to systematic quantitative analysis by classical data dependent proteomics methods (DDA). Moreover, DDA runs in shotgun proteomics experiments are plenty of missing values among the replicates due to the stochastic nature of the acquisition method, thus hampering the robustness of the quantitative analysis. Here, we have overcome these obstacles designing a robust workflow named missing value monitoring (MvM) in order to follow low abundance proteins dynamics.Cross-linking, in general, involves the covalent linkage of two amino acid residues of proteins or protein complexes in close proximity. Mass spectrometry and computational analysis are then applied to identify the formed linkage and deduce structural information such as distance restraints. Quantitative cross-linking coupled with mass spectrometry is well suited to study protein dynamics and conformations of protein complexes. The quantitative cross-linking workflow described here is based on the application of isotope labelled cross-linkers. Proteins or protein complexes present in different structural states are differentially cross-linked using a "light" and a "heavy" cross-linker. The intensity ratios of cross-links (i.e., light/heavy or heavy/light) indicate structural changes or interactions that are maintained in the different states. These structural insights lead to a better understanding of the function of the proteins or protein complexes investigated. The described workflow is applicable to a wide range of research questions including, for instance, protein dynamics or structural changes upon ligand binding.The use of stable isotope-labeled standards (SIS) is an analytically valid means of quantifying proteins in biological samples. The nature of the labele

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