Measuring community strength and social capital

Five case study communities in both metropolitan and regional urban locations in Australia are used as test sites to develop measures of 'community strength' on four domains: Natural Capital; Produced Economic Capital; Human Capital; and Social and Institutional Capital. The paper focuses on the fourth domain. Sample surveys of households in the five case study communities used a survey instrument with scaled items to measure four aspects of social capital - formal norms, informal norms, formal structures and informal structures - that embrace the concepts of trust, reciprocity, bonds, bridges, links and networks in the interaction of individuals with their community inherent in the notion social capital. Exploratory principal components analysis is used to identify factors that measure those aspects of social and institutional capital, while a confirmatory analysis based on Cronbach's alpha explores the robustness of the measures. Four primary scales and 15 subscales are identified when defining the domain of social and institutional capital. Further analysis reveals that two measures - anomie, and perceived quality of life and wellbeing - relate to certain primary scales of social capital.

Prediction of protein B-factor profiles

The polypeptide backbones and side chains of proteins are constantly moving due to thermal motion and the kinetic energy of the atoms. The B-factors of protein crystal structures reflect the fluctuation of atoms about their average positions and provide important information about protein dynamics. Computational approaches to predict thermal motion are useful for analyzing the dynamic properties of proteins with unknown structures. In this article, we utilize a novel support vector regression (SVR) approach to predict the B-factor distribution (B-factor profile) of a protein from its sequence. We explore schemes for encoding sequences and various settings for the parameters used in SVR. Based on a large dataset of high-resolution proteins, our method predicts the B-factor distribution with a Pearson correlation coefficient (CC) of 0.53. In addition, our method predicts the B-factor profile with a CC of at least 0.56 for more than half of the proteins. Our method also performs well for classifying residues (rigid vs. flexible). For almost all predicted B-factor thresholds, prediction accuracies (percent of correctly predicted residues) are greater than 70%. These results exceed the best results of other sequence-based prediction methods. (C) 2005 Wiley-Liss, Inc.