Ein Nachschlagewerk, das die urologischen Krankheitsbilder umfassend behandelt und dabei übersichtlich bleibt? Referenz Krankheitsbilder Urologie beweist, dass dies möglich ist: Gut verständlich und klar strukturiert liefert das Werk verlässliche Antworten auf die Fragestellungen zu urologischen Krankheitsbildern, Leitsymptomen und Methoden. Profitieren Sie von präzisen Angaben, wie Therapiealgorithmen oder Dosierungsempfehlungen, die Sie direkt im Arbeitsalltag anwenden können.

Hydration dynamics around proteins plays an important role in helping protein keep conformational stabilities and process biological functions. A good understanding of protein hydration is fundamental and significant to the development of protein science. In this thesis, we employ femtosecond-resolved fluorescence spectroscopy to study hydration dynamics of two interesting biological systems, gamma-M7-crystallin, and the GroE molecular chaperone system. Tryptophan site-directed mutagenesis is applied to achieve a single-residue spatial resolution. Furthermore, as tryptophan fluorescence can get quenched after excitation, a study of tryptophan fluorescence quenching mechanism was performed on gamma-M7 crystallin using both femtosecond-resolved fluorescence up-conversion and transient absorption methods. Gamma-M7-crystallin is an eye lens protein in zebrafish. Different from many other proteins, it has good solubility and stability under very high concentrations. Here, we studied its hydration dynamics under crowding conditions. Two typical sites are chosen, one exposed to the water and the other buried inside the protein. For the exposed probe under high concentration, we have observed a decrease in stabilization energy which mainly comes from expelling outer-layer water molecules as proteins come closer. Also, the solvation relaxations for these two mutants slowed down at high concentration but with different extents. This comes from the different amount of decreased outer-layer water. For the quenching study, we have done a single tryptophan mutation on nine locations on gamma-M7 with one unquenched mutant as control. The fluorescence up- conversion results support the appearance of a severe quenching besides solvation dynamics and give us a forward electron transfer time in tens to hundreds of picoseconds. We also performed femtosecond-resolved transient absorption measurements and captured the intermediate product (Trp*+) and resolved the backward electron transfer time. It is found that for most mutants backward electron transfer rate is slower than the forward one. The anisotropy results indicate a more flexible tryptophan sidechains in quenching tryptophan mutants. From molecular dynamics (MD) simulation results, we have figured out the most possible quencher around each tryptophan donor and calculated the coupling energy. GroE molecular chaperone system is a very large biological system helping to fold other proteins. It consists of two parts called GroEL and GroES, where GroEL provides a large cavity for protein folding and GroES works as a lid on it. We use femtosecond-resolved fluorescence spectroscopy to examine the hydration dynamics on the main GroEL cavity at the apical and equatorial domains. The results show that while the ultrafast hydration dynamics near the lid of the GroEL cavity are similar to bulk water, there is a significant slowdown of the ultrafast hydration dynamics at the bottom of the cavity. This result supports the active GroEL models that suggest the GroE system may affect substrate protein folding through water-mediated mechanisms.