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Characterisation of polyproline I secondary structure by means of vibrational and chiroptical spectroscopy methods and quantum mechanical simulations
Vančura, Martin ; Profant, Václav (advisor) ; Hudecová, Jana (referee)
Our investigation was focused on a secondary protein structure called polyproline I. This helical structure has been known for a long time, but its occurrence and significance in nature is not yet fully known. In this thesis, we use Raman spectroscopy and chiral sensitive Raman optical activity. These methods are sensitive to the structure of proteins but are more informative and sensitive to the local arrangement than the commonly used ECD and UV absorption. We were able to obtain polyproline I Raman and ROA spectra that have not yet been published. We have described important differences between the spectra of polyproline I and II and observed the process of mutarotation. The experimental part of the work is supplemented by quantum chemistry calculations of spectra using the transfer of molecular property tensor. The calculated spectra corresponded very well with the experimental spectra.
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Atomic force microscopy in the region of biomacromolecules
Vančura, Martin ; Kopecký, Vladimír (advisor) ; Bednárová, Lucie (referee)
Atomic force microscopy (AFM) enables sample imaging at the micro and nanoscale. Recently, the method is applied to investigate biomacromolecules. Here, we describe the basic principles of AFM with a special emphasis for bioapplications. We tested experimental abilities of Alpha 300 - the Raman microscope with AFM/SNOM accessory from WITec company. The ability of AFM to study objects of cellular dimensions was demonstrated on erythrocytes and green algae Desmodesmus quadricauda. We were able to observe growing of lysozyme protein fibrils on day scale - from dimensions of seeds (~3 nm height) up to fibrils itself (3-10 nm height and 100 nm up to micrometers length). Subsequently, we observed separate protein molecules of thyroglobulin (~6 nm) and also γ-globulin (~3 nm). It seems plausible to image objects up to 2 nm dimensions by the given device with respect to the signal/noise ratio.
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Characterisation of polyproline I secondary structure by means of vibrational and chiroptical spectroscopy methods and quantum mechanical simulations
Vančura, Martin ; Profant, Václav (advisor) ; Hudecová, Jana (referee)
Our investigation was focused on a secondary protein structure called polyproline I. This helical structure has been known for a long time, but its occurrence and significance in nature is not yet fully known. In this thesis, we use Raman spectroscopy and chiral sensitive Raman optical activity. These methods are sensitive to the structure of proteins but are more informative and sensitive to the local arrangement than the commonly used ECD and UV absorption. We were able to obtain polyproline I Raman and ROA spectra that have not yet been published. We have described important differences between the spectra of polyproline I and II and observed the process of mutarotation. The experimental part of the work is supplemented by quantum chemistry calculations of spectra using the transfer of molecular property tensor. The calculated spectra corresponded very well with the experimental spectra.
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Atomic force microscopy in the region of biomacromolecules
Vančura, Martin ; Kopecký, Vladimír (advisor) ; Bednárová, Lucie (referee)
Atomic force microscopy (AFM) enables sample imaging at the micro and nanoscale. Recently, the method is applied to investigate biomacromolecules. Here, we describe the basic principles of AFM with a special emphasis for bioapplications. We tested experimental abilities of Alpha 300 - the Raman microscope with AFM/SNOM accessory from WITec company. The ability of AFM to study objects of cellular dimensions was demonstrated on erythrocytes and green algae Desmodesmus quadricauda. We were able to observe growing of lysozyme protein fibrils on day scale - from dimensions of seeds (~3 nm height) up to fibrils itself (3-10 nm height and 100 nm up to micrometers length). Subsequently, we observed separate protein molecules of thyroglobulin (~6 nm) and also γ-globulin (~3 nm). It seems plausible to image objects up to 2 nm dimensions by the given device with respect to the signal/noise ratio.
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Evolution of phonological contrast in sibilants - typological analysis
Vančura, Martin ; Bičovský, Jan (advisor) ; Duběda, Tomáš (referee)
Martin Vančura - Diplomová práce (2012) Evolution of phonological contrat in sibilants - typological analysis Abstract: The goal of this paper is to employ the paradigm of Greenbergian language typology to process diachronic data originating in the field of historical linguistics. In the first few chapters, I discuss both disciplines and identify some of the pitfalls of such an endeavour. The substance of this paper lies in chapter 4 where I try to demonstrate a real utilization of this diachronic typology on a specific set of data, represented by documented cases of the evolution of sibilants. Then I analyse the precise articulatory and evolutionary character of the sibilants in selected branches of the Indo- European language family and selected languages of the world and I attempt to uncover the common evolutionary tendencies of their sibilant systems. At the end of this chapter, I construct a map of sibilants' evolutionary trajectories and I propose some remarks on the general phonetics and phonology of sibilants.
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