Influences of marital conflict on child adjustment: review of theory and research.

This review summarizes the literature on the relationship between marital conflict and child maladjustment with an emphasis on variables that qualify, explain the association, or both. Following a historical review, the modest findings on the strength of the association between marital conflict and child maladjustment is explored. The definition of marital conflict is clarified through specification of its various dimensions (frequency, intensity, content, resolution). The role of variables that serve to moderate and/or mediate the relationship between marital conflict and child maladjustment are elaborated. Mediating models include exposure theories (Modeling, Cognitive-Contextual effects: appraisal of threat and blame, and Emotional Insecurity) and changes in the parent-child relationship (Spillover). Variables that moderate or qualify the relationship include children's cognitions and behaviors, contextual factors, and demographic differences. A model is presented summarizing these mechanisms. Research recommendations are proposed and the clinical implications of this literature are addressed.

Detection of water proximity to tryptophan residues in proteins by single photon radioluminescence.

We recently developed a single photon radioluminescence (SPR) technique to measure submicroscopic distances in biological samples [Bicknese et al., and Shahrokh et al., Biophys. J., 63 (1992) 1256-1279]. SPR arises from the excitation of a fluorophore by the energy deposited from a slowing beta decay electron. The purpose of this study was to detect 3H2O molecules near tryptophan residues in proteins by tryptophan SPR. To detect small SPR signals, a sample compartment with reflective ellipsoidal optics was constructed, and amplified signals from a cooled photomultiplier were resolved by pulse-height analysis. A Monte Carlo calculation was carried out to quantify the relationship between SPR signal and 3H2O-tryptophan proximity. Measurements of tryptophan SPR were made on aqueous tryptophan; dissolved melittin (containing a single tryptophan); native and denatured aldolase; dissolved aldolase, monellin, and human serum albumin; and the integral membrane proteins CHIP28 (containing a putative aqueous pore) and MIP26 using 3H2O or the aqueous-phase probe 3H-3-O-methylglucose (OMG). After subtraction of a Bremsstrahlung background signal, the SPR signal from aqueous tryptophan (cps.microCi-1 mumol-1 +/- SE) was 8.6 +/- 0.2 with 3H2O and 7.8 +/- 0.3 with 3HOMG (n = 8). With 3H2O as donor, the SPR signal (cps.microCi-1 mumol-1) was 9.0 +/- 0.3 for monomeric melittin in low salt (trytophan exposed) and 4.6 +/- 0.8 (n = 9) for tetrameric melittin in high salt (tryptophans buried away from aqueous solution). The ratio of SPR signal obtained for aldolase under denaturing conditions of 8 M urea (fluorophores exposed) versus non-denaturing buffer (fluorophores buried) was 1.53 +/- 0.07 (n = 6). Ratios of SPR signals normalized to fluorescence intensities for monellin, aldolase, and human serum albumin, relative to that for d-tryptophan, were 1.42, 1.09, and 1.04, indicating that the cross-section for excitation of fluorophores in proteins is greater than that for tryptophan in solution. For the CHIP28 and MIP26 proteins in membranes, the ratio of SPR signal obtained with 3H2O versus 3HOMG was 1.35 +/- 0.13 (CHIP28, n = 5) and 0.99 +/- 0.02 (MIP26). These data are consistent with the existence of an aqueous channel through CHIP28 that excludes small solutes. We conclude that tryptophan radioluminescence in proteins is measurable and provides unique information about the presence of local aqueous compartments.

Calculation of resonance energy transfer in crowded biological membranes.

Analytical and numerical models were developed to describe fluorescence resonance energy transfer (RET) in crowded biological membranes. It was assumed that fluorescent donors were linked to membrane proteins and that acceptors were linked to membrane lipids. No restrictions were placed on the location of the donor within the protein or the partitioning of acceptors between the two leaflets of the bilayer; however, acceptors were excluded from the area occupied by proteins. Analytical equations were derived that give the average quantum yield of a donor at low protein concentrations. Monte Carlo simulations were used to generate protein and lipid distributions that were linked numerically with RET equations to determine the average quantum yield and the distribution of donor fluorescence lifetimes at high protein concentrations, up to 50% area fraction. The Monte Carlo results show such crowding always reduces the quantum yield, probably because crowding increases acceptor concentrations near donor-bearing proteins; the magnitude of the reduction increases monotonically with protein concentration. The Monte Carlo results also show that the distribution of fluorescence lifetimes can differ markedly, even for systems possessing the same average lifetime. The dependence of energy transfer on acceptor concentration, protein radius, donor position within the protein, and the fraction of acceptors in each leaflet was also examined. The model and results are directly applicable to the analysis of RET data obtained from biological membranes; their application should result in a more complete and accurate determination of the structures of membrane components.