Analysis of Donor Advised Funds from a Community Foundation Perspective

The Council of Michigan Foundations (CMF) commissioned four studies between 2000 and 2016 to evaluate the required private foundation payout rate as well as hypothetical model portfolios and actual investment returns.In December 2020, the Dorothy A. Johnson Center for Philanthropy (Johnson Center) at Grand Valley State University, in collaboration with Plante Moran Financial Advisors (PMFA), updated and expanded this research by using a comprehensive database of IRS Form 990-PF (private foundation) returns, adding international investments to the model portfolios, presenting actual payout rates of all private foundations in the dataset, and showing projections of how changes to the payout rate may affect future foundation assets. In March 2021, staff from the Johnson Center turned their focus to community foundations and completed a similar analysis — the first of its kind in the CMF foundation study series.Similar to its earlier private and community foundation report counterparts, this report provides new information to the field. To study donor advised funds (DAFs), the project team leveraged the Johnson Center's comprehensive database of IRS Form 990 filings for summary statistics. The team supplemented that dataset by partnering with CMF to obtain account-level information about the more than 2,600 DAFs housed at Michigan's community foundations. That account-level detail was used to calculate individual DAF investment returns, contribution and distribution flows, and payout rates for the years 2017–2020

Rational Generosity: The Indianapolis Foundation and the Community Foundation Response to the Great Depression

Indiana University-Purdue University Indianapolis (IUPUI)A historical analysis of the philanthropic response to the Great Depression by community foundations; the thesis uses the individual story of the Indianapolis Foundation as a case study to provide detailed examples of how community foundations modified their grant-making behavior in response to the Great Depression’s economic effects

The Henry Ford : sustaining Henry Ford's philanthropic legacy

Indiana University-Purdue University Indianapolis (IUPUI)This dissertation argues that the Edison Institute (presently known as The Henry Ford in Dearborn, Michigan) survived internal and external challenges through the evolution of the Ford family’s leadership and the organization’s funding strategy. Following Henry Ford’s death, the museum complex relied upon the Ford Foundation and the Ford Motor Company Fund as its sole means of philanthropic support. These foundations granted the Edison Institute a significant endowment, which it used to sustain its facilities in conjunction with its inaugural fundraising program. Navigating a changing legal, corporate, and philanthropic landscape in Detroit and around the world, the Ford family perpetuated Henry Ford’s legacy at the Edison Institute with the valuable guidance of executives and staff of their corporation, foundation, and philanthropies. Together they transitioned the Edison Institute into a sustainable and public nonprofit organization by overcoming threats related to the deaths of two generations of the Ford family, changes in the Edison Institute’s administration and organizational structure, the reorganization of the Ford Foundation, the effects of the Tax Reform Act of 1969, and legal complications due to overlap between the Fords’ corporate and philanthropic interests. The Ford family provided integral leadership for the development and evolution of the Edison Institute’s funding strategy and its relationship to their other corporate and philanthropic enterprises. The Institute’s management and funding can be best understood within the context of philanthropic developments of the Ford family during this period, including the formation of the Ford Foundation’s funding and concurrent activity.   This dissertation focuses on the research question of how the Edison Institute survived the Ford family’s evolving philanthropic strategy to seek a sustainable funding and management structure. The work examines its central research question over multiple chapters organized around the Ford family’s changing leadership at the Edison Institute, the increase of professionalized managers, and the Ford’s use of their corporation and philanthropies to provide integral support to the Edison Institute. In order to sustain the Edison Institute throughout the twentieth century, it adapted its operations to accommodate Henry Ford’s founding legacy, its legal environment, and the evolving practice of philanthropy in the United States

Identification of Channel-lining Amino Acid Residues in the Hydrophobic Segment of Colicin Ia

Colicin Ia is a bactericidal protein of 626 amino acid residues that kills its target cell by forming a channel in the inner membrane; it can also form voltage-dependent channels in planar lipid bilayer membranes. The channel-forming activity resides in the carboxy-terminal domain of ∼177 residues. In the crystal structure of the water-soluble conformation, this domain consists of a bundle of 10 α-helices, with eight mostly amphipathic helices surrounding a hydrophobic helical hairpin (helices H8-H9). We wish to know how this structure changes to form a channel in a lipid bilayer. Although there is evidence that the open channel has four transmembrane segments (H8, H9, and parts of H1 and H6-H7), their arrangement relative to the pore is largely unknown. Given the lack of a detailed structural model, it is imperative to better characterize the channel-lining protein segments. Here, we focus on a segment of 44 residues (573–616), which in the crystal structure comprises the H8-H9 hairpin and flanking regions. We mutated each of these residues to a unique cysteine, added the mutant colicins to the cis side of planar bilayers to form channels, and determined whether sulfhydryl-specific methanethiosulfonate reagents could alter the conduction of ions through the open channel. We found a pattern of reactivity consistent with parts of H8 and H9 lining the channel as α-helices, albeit rather short ones for spanning a lipid bilayer (12 residues). The effects of the reactions on channel conductance and selectivity tend to be greater for residues near the amino terminus of H8 and the carboxy terminus of H9, with particularly large effects for G577C, T581C, and G609C, suggesting that these residues may occupy a relatively constricted region near the cis end of the channel

Workplace Giving in Universities: A U.S. Case Study at Indiana University

The phenomenon of workplace giving is underexamined in the scholarly literature; philanthropic gifts by employees to their nonprofit employers have received less attention within national and transnational contexts. This study considered the association between university staff propensity toward “internal workplace giving” and donor characteristics, drawing on literature about organizational commitment and identification as a beginning for advancing theoretical understanding of employee–employer relationships and giving at both the micro-level and meso-level. The sample of 17,038 employees covered 3 years at Indiana University, an American, public, multicampus institution. Despite its specific national and cultural context, the study raises relevant issues about workplace giving. Relational and personal characteristics were found to be significant predictors for determining who donates; using these characteristics to predict giving levels, however, was less successful. The study anticipates a growing need for related research and provides direction for further methodological and theoretical approaches

Toolbox for analyzing finite two-state trajectories

In many experiments, the aim is to deduce an underlying multi-substate on-off kinetic scheme (KS) from the statistical properties of a two-state trajectory. However, the mapping of a KS into a two-state trajectory leads to the loss of information about the KS, and so, in many cases, more than one KS can be associated with the data. We recently showed that the optimal way to solve this problem is to use canonical forms of reduced dimensions (RD). RD forms are on-off networks with connections only between substates of different states, where the connections can have non-exponential waiting time probability density functions (WT-PDFs). In theory, only a single RD form can be associated with the data. To utilize RD forms in the analysis of the data, a RD form should be associated with the data. Here, we give a toolbox for building a RD form from a finite two-state trajectory. The methods in the toolbox are based on known statistical methods in data analysis, combined with statistical methods and numerical algorithms designed specifically for the current problem. Our toolbox is self-contained - it builds a mechanism based only on the information it extracts from the data, and its implementation on the data is fast (analyzing a 10^6 cycle trajectory from a thirty-parameter mechanism takes a couple of hours on a PC with a 2.66 GHz processor). The toolbox is automated and is freely available for academic research upon electronic request

Sizing the Protein Translocation Pathway of Colicin Ia Channels

The bacterial toxin colicin Ia forms voltage-gated channels in planar lipid bilayers. The toxin consists of three domains, with the carboxy-terminal domain (C-domain) responsible for channel formation. The C-domain contributes four membrane-spanning segments and a 68-residue translocated segment to the open channel, whereas the upstream domains and the amino-terminal end of the C-domain stay on the cis side of the membrane. The isolated C-domain, lacking the two upstream domains, also forms channels; however, the amino terminus and one of the normally membrane-spanning segments can move across the membrane. (This can be observed as a drop in single-channel conductance.) In longer carboxy-terminal fragments of colicin Ia that include ≤169 residues upstream from the C-domain, the entire upstream region is translocated. Presumably, a portion of the C-domain creates a pathway for the polar upstream region to move through the membrane. To determine the size of this translocation pathway, we have attached “molecular stoppers,” small disulfide-bonded polypeptides, to the amino terminus of the C-domain, and determined whether they could be translocated. We have found that the translocation rate is strongly voltage dependent, and that at voltages ≥90 mV, even a 26-Å stopper is translocated. Upon reduction of their disulfide bonds, all of the stoppers are easily translocated, indicating that it is the folded structure, rather than some aspect of the primary sequence, that slows translocation of the stoppers. Thus, the pathway for translocation is ≥26 Å in diameter, or can stretch to this value. This is large enough for an α-helical hairpin to fit through

Correctly validating results from single molecule data: the case of stretched exponential decay in the catalytic activity of single lipase B molecules

The question of how to validate and interpret correctly the waiting time probability density functions (WT-PDFs) from single molecule data is addressed. It is shown by simulation that when a stretched exponential WT-PDF, with a stretched exponent alfa and a time scale parameter tau, generates the off periods of a two-state trajectory, a reliable recovery of the input WT-PDF from the trajectory is obtained even when the bin size used to define the trajectory, dt, is much larger than the parameter tau. This holds true as long as the first moment of the WT-PDF is much larger than dt. Our results validate the results in an earlier study of the activity of single Lipase B molecules and disprove recent related critique