Global ETD Search

1	Quantitative Mass Spectrometric Analysis of RNA-Protein Cross-Links Qamar, Saadia 02 March 2020 (has links) No description available. 570 Proteomics Mass spectrometry RNA-protein cross-linking RNP complexes Biologie (PPN619462639)
2	A Study of Penicillin Binding Proteins in Mycobacterium Tuberculosis Anderson, Lisa Louise 11 October 2001 (has links) No description available. Chemistry, Biochemistry Penicillin Binding Proteins Cyanogen Mycobacterium Tuberculosis Cell Wall-Synthesizing Complex Protein Cross-Linking
3	Development of chromogenic cross-linkers and selective gas-phase dissociation methods to assess protein macromolecular structures by mass spectrometry Gardner, Myles Winston 05 August 2010 (has links) Selective gas-phase dissociation strategies have been developed for the characterization of cross-linked peptides and proteins in quadrupole ion trap mass spectrometers. An infrared chromogenic cross-linker (IRCX) containing a phosphotriester afforded rapid differentiation of cross-linked peptides from unmodified ones in proteolytic digests of cross-linked proteins by selective infrared multiphoton dissociation (IRMPD). Only the cross-linked peptides containing the chromogenic phosphate underwent IRMPD and unmodified peptides were not affected by IR irradiation. IRMPD of IRCX-cross-linked peptides yielded uncross-linked y-ion sequence tags of the constituent peptides due to secondary dissociation of all primary product ions which contained the chromophore, thus allowing successful de novo sequencing of the cross-linked peptides. Peptides cross-linked via a two-step conjugation strategy through the formation of a bis-arylhydrazone (BAH) bond were selectively dissociated by ultraviolet radiation at 355 nm. The BAH-cross-linked peptides could be distinguished from not only unmodified peptides but also dead-end modified peptides based on the selectivity of ultraviolet photodissociation. In a complementary approach, electron transfer dissociation of BAH-cross-linked peptides resulted in preferential cleavage of the hydrazone bond which produced two modified peptides. These modified peptides were subsequently interrogated by CID which allowed for the original site of cross-linking to be pinpointed. IRMPD was implemented in a dual pressure linear ion trap to demonstrate successful photodissociation of peptides having modest absorptivities. Peptides were observed to efficiently dissociation by IR irradiation exclusively in the low pressure cell whereas no dissociation was observed in the high pressure cell due to extensive collisional cooling. IRMPD provided greater sequence coverage of the peptides than CID and yielded product ion mass spectra which were predominantly composed of singly charged product ions which simplified spectral interpretation. IRMPD was further applied for the sequencing of small-interfering RNA. Complete sequence coverage was obtained and the results were compared to CID. / text Mass spectrometry Infrared multiphoton dissociation Cross-linking Quadrupole ion trap Photodissociation Protein cross-linking Electron transfer dissociation Ultraviolet photodissociation Small-interfering RNA
4	Investigation of prokaryotic immune defense system with quantitative and structural mass spectrometry Sharma, Kundan 29 April 2015 (has links) No description available. 570 Prokaryotic Immune Defense CRISPR-Cas Mass Spectrometry Structural proteomics Protein-RNA cross-linking Protein-Protein cross-linking Quantitative proteomics iBAQ Dimethyl labeling Biologie (PPN619462639)
5	Size Separation Techniques for the Characterisation of Cross-Linked Casein: A Review of Methods and Their Applications Raak, Norbert, Abbate, Raffaele Andrea, Lederer, Albena, Rohm, Harald, Jaros, Doris 11 June 2018 (has links) Casein is the major protein fraction in milk, and its cross-linking has been a topic of scientific interest for many years. Enzymatic cross-linking has huge potential to modify relevant techno-functional properties of casein, whereas non-enzymatic cross-linking occurs naturally during the storage and processing of milk and dairy products. Two size separation techniques were applied for characterisation of these reactions: gel electrophoresis and size exclusion chromatography. This review summarises their separation principles and discusses the outcome of studies on cross-linked casein from the last ~20 years. Both methods, however, show limitations concerning separation range and are applied mainly under denaturing and reducing conditions. In contrast, field flow fractionation has a broad separation range and can be easily applied under native conditions. Although this method has become a powerful tool in polymer and nanoparticle analysis and was used in few studies on casein micelles, it has not yet been applied to investigate cross-linked casein. Finally, the principles and requirements for absolute molar mass determination are reviewed, which will be of increased interest in the future since suitable calibration substances for casein polymers are scarce. info:eu-repo/classification/ddc/540 ddc:540
6	The Development and Application of Mass Spectrometry-based Structural Proteomic Approaches to Study Protein Structure and Interactions Makepeace, Karl A.T. 26 August 2022 (has links) Proteins and their intricate network of interactions are fundamental to many molecular processes that govern life. Mass spectrometry-based structural proteomics represents a powerful set of techniques for characterizing protein structures and interactions. The last decade has witnessed a large-scale adoption in the application of these techniques toward solving a variety of biological questions. Addressing these questions has often been coincident with the further development of these techniques. Insight into the structures of individual proteins and their interactions with other proteins in a proteome-wide context has been made possible by recent developments in the relatively new field of chemical crosslinking combined with mass spectrometry. In these experiments crosslinking reagents are used to capture protein-protein interactions by forming covalent linkages between proximal amino acid residues. The crosslinked proteins are then enzymatically digested into peptides, and the covalently-coupled crosslinked peptides are identified by mass spectrometry. These identified crosslinked peptides thus provide evidence of interacting regions within or between proteins. In this dissertation the development of tools and methods that facilitate this powerful technique are described. The primary arc of this work follows the development and application of mass spectrometry-based approaches for the identification of protein crosslinks ranging from those which exist endogenously to those which are introduced synthetically. Firstly, the development of a novel strategy for comprehensive determination of naturally occurring protein crosslinks in the form of disulfide bonds is described. Secondly, the application of crosslinking reagents to create synthetic crosslinks in proteins coupled with molecular dynamics simulations is explored in order to structurally characterize the intrinsically disordered tau protein. Thirdly, improvements to a crosslinking-mass spectrometry method for defining a protein-protein interactome in a complex sample is developed. Altogether, these described approaches represent a toolset to allow researchers to access information about protein structure and interactions. / Graduate Mass Spectrometry Structural Proteomics Crosslinking Cross-linking Disulfide bonds Proteomics Tau Mitochondria Method development Molecular dynamics Protein chemistry Protein crosslinking Protein cross-linking Shotgun proteomics Bottom-up proteomics Data-dependent acquisition DDA Protein-protein interactome Interactome Interactomics Proteinase K Trypsin Higher-order crosslinking Machine learning Feature engineering Yeast Yeast mitochondria Algorithms Data analysis Surface modification Molecular modelling Non-specific digest Structural mass spectrometry Structural biology Biochemistry LC-MS

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