58 research outputs found
Emerging Microfluidic Approaches for Platelet Mechanobiology and Interplay With Circulatory Systems
Understanding how platelets can sense and respond to hemodynamic forces in disturbed blood flow and complexed vasculature is crucial to the development of more effective and safer antithrombotic therapeutics. By incorporating diverse structural and functional designs, microfluidic technologies have emerged to mimic microvascular anatomies and hemodynamic microenvironments, which open the floodgates for fascinating platelet mechanobiology investigations. The latest endothelialized microfluidics can even recapitulate the crosstalk between platelets and the circulatory system, including the vessel walls and plasma proteins such as von Willebrand factor. Hereby, we highlight these exciting microfluidic applications to platelet mechanobiology and platelet–circulatory system interplay as implicated in thrombosis. Last but not least, we discuss the need for microfluidic standardization and summarize the commercially available microfluidic platforms for researchers to obtain reproducible and consistent results in the field.</jats:p
Simulations of two-dimensional infrared and stimulated resonance Raman spectra of photoactive yellow protein
We present simulations of one and two-dimensional infrared (2DIR) and stimulated resonance Raman (SRR) spectra of the dark state (pG) and early red-shifted intermediate (pR) of photoactive yellow protein (PYP). Shifts in the amide I and Glu46 COOH stretching bands distinguish between pG and pR in the IR absorption and 2DIR spectra. The one-dimensional SRR spectra are similar to the spontaneous RR spectra. The two-dimensional SRR spectra show large changes in cross peaks involving the C=O stretch of the two species and are more sensitive to the chromophore structure than 2DIR spectra
Study of the 10B(p,αγ)7Be and 10B(p,p'γ)10B reactions for PIGE purposes
Εθνικό Μετσόβιο Πολυτεχνείο--Μεταπτυχιακή Εργασία. Διεπιστημονικό-Διατμηματικό Πρόγραμμα Μεταπτυχιακών Σπουδών (Δ.Π.Μ.Σ.) “Φυσική και Τεχνολογικές Εφαρμογές
Study of the reaction 32S (p,p'g) 32S in the energy range 3-4 MeV.
63 σ.Η παρούσα εργασία έγινε στα πλαίσια εκπόνησης της διπλωματικής εργασίας του προπτυχιακού φοιτητή της Σχολής Εφαρμοσμένων Μαθηματικών και Φυσικών
Επιστημών του Ε.Μ.Π., Πρεκετέ-Σιγάλα Κωνσταντίνου. Αφορά στον υπολογισμό της διαφορικής ενεργού διατομής της αντίδρασης 32S(p,p’γ)32S στο ενεργειακό εύρος των 3-4 MeV και σε γωνίες 0˚, 15˚, 55˚, 90˚, 125˚ και 155˚. Η αντίδραση αυτή έχει μελετηθεί και στο παρελθόν από άλλες ερευνητικές ομάδες, αλλά σε λιγότερο αριθμό γωνιών και με μεγαλύτερη αβεβαιότητα αυτών, και επίσης υπάρχει ασυμφωνία στις
ενέργειες που παρουσιάζονται οι συντονισμοί, καθώς και στις εντάσεις τους. Η ακρίβεια αυτών των τιμών είναι σημαντική, γιατί ελαφριά στοιχεία, όπως το θείο, απασχολούν αρκετές εφαρμογές της τεχνικής PIGE. Το πείραμα εκτελέστηκε στο εργαστήριο του ηλεκτροστατικού επιταχυντή, TANDEM, του Ι.Π.Σ.Φ. του Ε.Κ.Ε.Φ.Ε.
“Δημόκριτος”.This work was done in preparation of the thesis of the undergraduate student of the School of Applied Mathematical and Physical Sciences, N.T.U.A., Preketes-Sigalas Konstantinos. It is about the calculation of the differential cross sections of the reaction 32S(p,p'g)32S in the energy range of 3-4 MeV and at angles of 0˚, 15˚, 55˚, 90˚, 125˚ and 155˚. This reaction has been studied in the past by other research groups, but in less number of angles and greater uncertainties, and there is also a mismatch effects in the resonances, and the intensity. The accuracy of these values is important because light elements, such as sulfur, present in several applications of the technique PIGE. The experiment was performed in the laboratory of electrostatic accelerator, TANDEM, the I.N.P.P. of N.C.S.R. "Demokritos".Κωνσταντίνος Α. Πρεκετές-Σιγάλα
J. Lawrence Buell, Mrs. J. Lawrence Buell, H. Glenn Bixby, Harold Shapiro, Mrs. Harold Shapiro (image)
Autumn Issuehttp://deepblue.lib.umich.edu/bitstream/2027.42/61100/1/1303.pd
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Simulations of Two-dimensional Infrared and Stimulated Resonance Raman Spectra of Photoactive Yellow Protein.
We present simulations of one and two-dimensional infrared (2DIR) and stimulated resonance Raman (SRR) spectra of the dark state (pG) and early red-shifted intermediate (pR) of photoactive yellow protein (PYP). Shifts in the amide I and Glu46 COOH stretching bands distinguish between pG and pR in the IR absorption and 2DIR spectra. The one-dimensional SRR spectra are similar to the spontaneous RR spectra. The two-dimensional SRR spectra show large changes in cross peaks involving the C=O stretch of the two species and are more sensitive to the chromophore structure than 2DIR spectra
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