¹⁹F NMR as a tool in chemical biology

• Diana Gimenez,
• Aoife Phelan,
• Cormac D. Murphy and
• Steven L. Cobb

Beilstein J. Org. Chem. 2021, 17, 293–318, doi:10.3762/bjoc.17.28

• are being investigated that enable the enzymatic post-translational modification of non-nucleophilic residues, such as glutamate [31]. As recently demonstrated by Kojima and co-workers, recombinant protein transglutaminase (TGase) could be used to catalyse the chemical replacement of the γ

GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

• Toan K. Phung,
• Cassandra L. Pegg and
• Benjamin L. Schulz

Beilstein J. Org. Chem. 2020, 16, 2127–2135, doi:10.3762/bjoc.16.180

• -glycosylation; O-glycosylation; Python; Introduction Glycosylation is a key post-translational modification critical for protein folding and function in eukaryotes [1][2][3]. Diverse types of glycosylation are known, all involving modification of specific amino acid residues with complex carbohydrate

Synthesis of new asparagine-based glycopeptides for future scanning tunneling microscopy investigations

• Laura Sršan and
• Thomas Ziegler

Beilstein J. Org. Chem. 2020, 16, 888–894, doi:10.3762/bjoc.16.80

• pathogenesis [1][2][3][4]. Glycosylation is also considered to be one of the most important post-translational modification (PTM) since more than half of all human proteins are glycopeptides or glycoproteins [5]. Therefore, understanding how glycopeptides interact on an intra- and intermolecular level is

Strategies toward protecting group-free glycosylation through selective activation of the anomeric center

• A. Michael Downey and
• Michal Hocek

Beilstein J. Org. Chem. 2017, 13, 1239–1279, doi:10.3762/bjoc.13.123

• ; Review 1 Introduction The glycosylation reaction is of extreme importance in nature as it is possibly the most prevalent post-translational modification and thus has implications in a tremendous number of biological processes, including diseases [1]. More expedient chemical and enzymatic methods to

Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience

• Serge Pérez and
• Daniele de Sanctis

Beilstein J. Org. Chem. 2017, 13, 1145–1167, doi:10.3762/bjoc.13.114

• glycosylated, whereas proteins expressed in E. coli do not contain any glycan chains. For proteins that require post-translational modification, eukaryotic expression systems are usually preferred [30]. The crystallization of glycoproteins faces several obstacles, including the micro-heterogenity of glycans at

Posttranslational isoprenylation of tryptophan in bacteria

• Masahiro Okada,
• Tomotoshi Sugita and
• Ikuro Abe

Beilstein J. Org. Chem. 2017, 13, 338–346, doi:10.3762/bjoc.13.37

• ; isoprenylation; post-translational modification; quorum sensing; tryptophan; Introduction Posttranslational modification is the chemical modification of proteins after their translation from mRNAs to the corresponding polypeptide chains synthesized by ribosomes. Since a posttranslational modification generates

• . Therefore, posttranslational modifications dynamically regulate the biological activities of proteins. Novel modifications have been discovered over the last several decades, revealing numerous post-translational modification patterns, including isoprenylation [1][2]. This review will discuss the

From supramolecular chemistry to the nucleosome: studies in biomolecular recognition

• Marcey L. Waters

Beilstein J. Org. Chem. 2016, 12, 1863–1869, doi:10.3762/bjoc.12.175

• -helices; aromatic interactions; β-hairpin peptides; cation–π interactions; dynamic combinatorial chemistry; histone; molecular recognition in water; nucleosome; π–π-stacking; post-translational modification; supramolecular chemistry; Review Childhood influences When thinking about how to start writing

• structure of a protein that binds to trimethyllysine (KMe3), an important post-translational modification involved in controlling gene expression, shows that it recognizes the trimethylammonium group via an aromatic cage (Figure 6a) [39]. This suggests that the binding is driven by cation–π interactions. We

Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides

• Andrew W. Truman

Beilstein J. Org. Chem. 2016, 12, 1250–1268, doi:10.3762/bjoc.12.120

• predictably than molecules made from multi-domain megasynthases such as polyketides and non-ribosomal peptides. Cyclisation is a common post-translational modification in RiPP pathways and includes a multitude of transformations. These modifications are usually essential for the proper biological activity of

Profluorescent substrates for the screening of olefin metathesis catalysts

• Raphael Reuter and
• Thomas R. Ward

Beilstein J. Org. Chem. 2015, 11, 1886–1892, doi:10.3762/bjoc.11.203

• recent applications, metathesis has also been used in chemical biology, either in the form of an artificial metalloenzyme [8][9][10] or for the post-translational modification of proteins [11]. To address these various challenges, a vast number of carbene complexes based on different transition metals

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• in microorganisms Microbial natural products of the peptide class are produced by two types of biosynthetic pathways: By giant multi-domain enzymes, the nonribosomal peptide synthetases (NRPS) or by ribosomal synthesis and subsequent post-translational modification and processing. NRPS consist of

• and a core peptide. Associated post-translational modification enzymes (PTMs) catalyze different types of macrocyclizations of the core peptide and side-chain modifications of amino acids. Peptide maturation further requires cleavage of the leader peptide by processing proteases (PP) frequently

• Microcystis and Planktothrix [64][65]. Post-translational modification of microviridins is achieved by the activity of two closely related ATP grasp ligases, MdnB and MdnC (MvdC and D in Planktothrix). The enzymes introduce two ω-ester linkages between threonine and aspartate and serine and glutamate (MdnC

Synthesis of glycosylated β³-homo-threonine conjugates for mucin-like glycopeptide antigen analogues

• Florian Karch and
• Anja Hoffmann-Röder

Beilstein J. Org. Chem. 2010, 6, No. 47, doi:10.3762/bjoc.6.47

• increased biological half-life. Keywords: glycopeptide; glycosylamino acids; β3-homo-threonine; MUC1 antigens; solid-phase synthesis; Introduction Glycosylation is the predominant co- and post-translational modification in higher organisms responsible for tailoring and fine-tuning of the activity of