Fluorescence quenching studies with proteins.

The enthalpy of dilution of all one-and two-solute aqueous mixtures of a series of compounds were measured from about 0.2 to 2.0 mole-kg−1 at 25°C. The compounds included in the study wereN-methylformamide,N-methylacetamide,N-methylpropionamide,N-butylacetamide, urea, ethylene glycol, pentaerythritol, glucose, and sucrose. The results of the enthalpy measurements were used to calculate the pairwise enthalpy of interaction for each compound with all the other compounds. A simple additivity principle is used to correlate the data. The principle assumes that each functional group on one molecule interacts with every functional group on the other molecule and that each of these interactions has a characteristic effect on the enthalpy that is independent of the positions of the functional groups in the two molecules. The resulting equation gives a rough but useful correlation of the results. Of the six interactions between the CH2, CONH, and CHOH functional groups, the CONH−CONH interaction is the strongest, the CHOH−CHOH interaction is the weakest, and the CH2−CH2 interaction is about equal in magnitude to the rest of the interactions. Thus, the CH2−CH2 and CONH−CONH are not the only interactions making important contributions to the enthalpy of a wide variety of systems.

Enthalpy of dilution of aqueous mixtures of amides, sugars, urea, ethylene glycol, and pentaerythritol at 25°C: Enthalpy of interaction of the hydrocarbon, amide, and hydroxyl functional groups in dilute aqueous solutions

Publisher Summary This chapter considers various ways of presenting and interpreting data using model calculations based on the modified Stern–Volmer equation. It provides detail information about the experimental methods for the purpose of obtaining meaningful quenching data. A quencher molecule can deactivate an excited fluorophor at the instant of excitation by forming a nonfluorescent, or “dark,” complex in the ground state, or by being present within a certain “sphere of action” at the time of excitation. Before considering heterogeneous systems, certain effects that can cause deviations from the simple Stem–Volmer law are also described in the chapter. Solute quenching of protein fluorescence is a technique that can yield information regarding the exposure of protein-bound intrinsic or extrinsic fluorophors. It is a dynamic method, because the presence of solute alters the fluorescence lifetime and thereby the steady-state intensity, without altering the electronic energy levels that are involved.

Solute quenching of protein fluorescence.

Chromatographic hydrophobic parameters in correlation analysis of structure-activity relationships.

It is frequently advantageous to consider the evolution of ideas and results when surveying a particular area of reseach since the early results often contain the fundamental outlines of a problem which subsequently become obscured by the later accumulation of detailed knowledge The history of the development of protein fluorescence followed a logical pattern and so is quite suitable to discuss with a linear time scale Because there are many experimental complications presented to investigators of the luminescence of biological macromolecules, each advance in knowledge was and is intimately associated with technological breakthroughs in measurement rather than with advances in theory Also, because of considerable inherent difficulties in luminescence measurements, many of the initial observations announced were later shown to be in error So, with apologies to friends and former colleagues for remembering the errors, it is hoped that a brief account of the development of the field will prove to be of value to those who are tempted to enter this difficult area, which is one so susceptible to serious errors

Luminescence of Polypeptides and Proteins

Thermodynamic Data from Fluorescence Spectra. I. The System Phenol-Acetate1

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Thermodynamic Data from Fluorescence Spectra. I. The System Phenol-Acetate1