![]() ![]() Anal Chem 75(3):663–670.Chapter 2: Protein Structure 2.1 Amino Acid Structure and Properties 2.2 Peptide Bond Formation and Primary Protein Structure 2.3 Secondary Protein Structure 2.4 Supersecondary Structure and Protein MotifsĢ.5 Tertiary and Quaternary Protein Structure 2.6 Protein Folding, Denaturation and Hydrolysis 2.7 References Rappsilber J, Ishihama Y, Mann M (2003) Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Reichardt S, Repper D, Tuzhikov AI, Galiullina RA, Planas-Marques M, Chichkova NV, Vartapetian AB, Stintzi A, Schaller A (2018) The tomato subtilase family includes several cell death-related proteinases with caspase specificity. (97)00523-2īeloshistov RE, Dreizler K, Galiullina RA, Tuzhikov AI, Serebryakova MV, Reichardt S, Shaw J, Taliansky ME, Pfannstiel J, Chichkova NV, Stintzi A, Schaller A, Vartapetian AB (2018) Phytaspase-mediated precursor processing and maturation of the wound hormone systemin. Schaller A (1998) Action of proteolysis-resistant systemin analogues in wound signalling. Liu B, Schofield CJ, Wilmouth RC (2006) Structural analyses on intermediates in serine protease catalysis. īizzozero SA, Dutler H (1981) Stereochemical aspects of peptide hydrolysis catalyzed by serine proteases of the chymotrypsin type. Syrén P-O, Hult K (2011) Amidases have a hydrogen bond that facilitates nitrogen inversion, but esterases have not. Syrén P-O (2018) Enzymatic hydrolysis of tertiary amide bonds by anti nucleophilic attack and protonation. Vagner J, Qu H, Hruby VJ (2008) Peptidomimetics, a synthetic tool of drug discovery. Grauer A, König B (2009) Peptidomimetics-a versatile route to biologically active compounds. Reichardt S, Piepho H-P, Stintzi A, Schaller A (2020) Peptide signaling for drought-induced tomato flower drop. Stührwohldt N, Ehinger A, Thellmann K, Schaller A (2020) Processing and formation of bioactive CLE40 peptide are controlled by posttranslational proline hydroxylation. Ghorbani S, Hoogewijs K, Pečenková T, Fernandez A, Inzé A, Eeckhout D, Kawa D, De Jaeger G, Beeckman T, Madder A, Van Breusegem F, Hilson P (2016) The SBT6.1 subtilase processes the GOLVEN1 peptide controlling cell elongation. Schardon K, Hohl M, Graff L, Schulze W, Pfannstiel J, Stintzi A, Schaller A (2016) Precursor processing for plant peptide hormone maturation by subtilisin-like serine proteinases. Overall CM, Blobel CP (2007) In search of partners: linking extracellular proteases to substrates. Van Der Hoorn RAL (2008) Plant proteases: from phenotypes to molecular mechanisms. Schaller A (2004) A cut above the rest: the regulatory function of plant proteases. Stührwohldt N, Schaller A (2019) Regulation of plant peptide hormones and growth factors by post-translational modification. Schaller A, Stintzi A, Rivas S, Serrano I, Chichkova NV, Vartapetian AB, Martínez D, Guiamét JJ, Sueldo DJ, van der Hoorn RAL, Ramírez V, Vera P (2018) From structure to function-a family portrait of plant subtilases. This can be accomplished with the MALDI-TOF mass spectrometry-based assay we describe here. For this approach, it is important to show that modification of the peptide backbone has the desired effect and does indeed protect the respective peptide bond against proteolysis. Peptide backbone modifications have been employed to increase the metabolic stability of peptide drugs, and in basic research, to investigate whether processing at a certain site is required for precursor maturation and formation of the bioactive peptide. Peptide-based bioassays have the distinctive advantage that peptides can be protected against proteolytic cleavage by backbone modifications, i.e., without changing the amino acid sequence. In genetic complementation experiments, site-directed mutagenesis has to be used to mask a processing site against proteolysis. Similarly, cleavable and non-cleavable synthetic peptides can be used in bioassays to test whether processing is required for bioactivity. The physiological relevance of site-specific precursor processing for the biogenesis of peptide hormones and growth factors can be demonstrated in genetic complementation experiments, in which a gain of function is observed for the cleavable wild-type precursor, but not for a non-cleavable precursor mutant. ![]()
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