The social scientific analysis of social class is attracting renewed interest given the accentuation of economic and social inequalities throughout the world. The most widely validated measure of social class, the Nuffield class schema, developed in the 1970s, was codified in the UK’s National Statistics Socio-Economic Classification (NS-SEC) and places people in one of seven main classes according to their occupation and employment status. This principally distinguishes between people working in routine or semi-routine occupations employed on a ‘labour contract’ on the one hand, and those working in professional or managerial occupations employed on a ‘service contract’ on the other. However, this occupationally based class schema does not effectively capture the role of social and cultural processes in generating class divisions. We analyse the largest survey of social class ever conducted in the UK, the BBC’s 2011 Great British Class Survey, with 161,400 web respondents, as well as a nationally representative sample survey, which includes unusually detailed questions asked on social, cultural and economic capital. Using latent class analysis on these variables, we derive seven classes. We demonstrate the existence of an ‘elite’, whose wealth separates them from an established middle class, as well as a class of technical experts and a class of ‘new affluent’ workers. We also show that at the lower levels of the class structure, alongside an ageing traditional working class, there is a ‘precariat’ characterised by very low levels of capital, and a group of emergent service workers. We think that this new seven class model recognises both social polarisation in British society and class fragmentation in its middle layers, and will attract enormous interest from a wide social scientific community in offering an up-to-date multi-dimensional model of social class.

Circular Dichroism (CD) spectroscopy is a long-established technique for studying protein secondary structures in solution. Empirical analyses of CD data rely on the availability of reference datasets comprised of far-UV CD spectra of proteins whose crystal structures have been determined. This article reports on the creation of a new reference dataset which effectively covers both secondary structure and fold space, and uses the higher information content available in synchrotron radiation circular dichroism (SRCD) spectra to more accurately predict secondary structure than has been possible with existing reference datasets. It also examines the effects of wavelength range, structural redundancy and different means of categorizing secondary structures on the accuracy of the analyses. In addition, it describes a novel use of hierarchical cluster analyses to identify protein relatedness based on spectral properties alone. The databases are shown to be applicable in both conventional CD and SRCD spectroscopic analyses of proteins. Hence, by combining new bioinformatics and biophysical methods, a database has been produced that should have wide applicability as a tool for structural molecular biology.

CDtool is a software package written to facilitate circular dichroism (CD) spectroscopic studies on both conventional lab-based instruments and synchrotron beamlines. It takes format-independent input data from any type of CD instrument, enables a wide range of standard and advanced processing methods, and, in a single user-friendly graphics-based package, takes raw data through the entire processing procedure and, importantly, uses data-mining techniques to retain in the final output all the information associated with the processing. It permits the facile comparison of data obtained from different instruments without the need for reformatting and displays it in graphical formats suitable for publication. It also includes the ability to automatically archive the processed data. This latter feature may be especially useful in light of recent funding institution directives with regard to data sharing and archiving and requirements for ''good practice'' and ''traceability'' within the pharmaceutical industry. In addition, CDtool includes a means of interfacing with protein data bank coordinate files and calculating secondary structures from them using alternate definitions and algorithms. This feature, along with a function that permits the facile production of new reference databases, enables the creation of specialized databases for secondary structural analyses of specific types of proteins. Thus the CDtool software not only enables rapid data processing and analyses but also includes many enhanced features not available in other CD data processing/analysis packages. Ó 2004 Elsevier Inc. All rights reserved.Keywords: Circular dichroism spectroscopy; Synchrotron radiation circular dichroism (SRCD); Archive; Data processing; Software; PDB Rapid data collection is one of the advantages of using circular dichroism (CD) spectroscopy for the analysis of protein structures. It is the subsequent data processing and analysis steps that can be surprisingly time consuming. This discrepancy becomes even more acute for synchrotron radiation-based circular dichroism (SRCD) 1 spectra, which can be accumulated on a very short timescale.Currently several different software packages are required for processing, comparing, and analyzing CD data. Data collection and some processing software are usually supplied with commercial CD instruments and each SRCD beamline has developed its own data collection software. The data processing functions from the various instruments tend to differ considerably, which makes cross-instrument processing of data, and thus comparisons, extremely difficult. To surmount these problems in the past, a very simple generic program (SUPER3) was developed to include a range of processing functions [1] and simple analyses, but this software does not now adequately meet the needs of ever more sophisticated data collection procedures.Analysis tools developed for CD spectra include a wide range of secondary structure calculation algorithms [2-6] which often require reformatting, rescaling, and other man...

This paper responds to the critical reception of the arguments made about social class in Savage et al (2013). It emphasises the need to disentangle different strands of debate so as not to conflate four separate issues, (a) the value of the seven class model proposed; (b) the potential of the large web survey-the Great British Class Survey (GBCS) for future research; (c) the value of Bourdieusian perspectives for re-energising class analysis, and (d) the academic and public reception to the GBCS itself. We argue that in order to do justice to its full potential, we need a concept of class which does not reduce it to a technical measure of a single variable and which recognises how multiple axes of inequality can crystallise as social classes. Whilst recognising the limitations of what we are able to claim on the basis of the GfK/GBCS, we argue that the seven classes defined in Savage et al (2013) have sociological resonance in pointing to the need to move away from a focus on class boundaries at the middle reaches of the class structure towards an analysis of the power of elite formation.

Circular dichroism (CD) spectroscopy is a valuable method for defining canonical secondary structure contents of proteins based on empirically-defined spectroscopic signatures derived from proteins with known three-dimensional structures. Many proteins identified as being "Intrinsically Disordered Proteins" have a significant amount of their structure that is neither sheet, helix, nor turn; this type of structure is often classified by CD as "other", "random coil", "unordered", or "disordered". However the "other" category can also include polyproline II (PPII)-type structures, whose spectral properties have not been well-distinguished from those of unordered structures. In this study, synchrotron radiation circular dichroism spectroscopy was used to investigate the spectral properties of collagen and polyproline, which both contain PPII-type structures. Their native spectra were compared as representatives of PPII structures. In addition, their spectra before and after treatment with various conditions to produce unfolded or denatured structures were also compared, with the aim of defining the differences between CD spectra of PPII and disordered structures. We conclude that the spectral features of collagen are more appropriate than those of polyproline for use as the representative spectrum for PPII structures present in typical amino acid-containing proteins, and that the single most characteristic spectroscopic feature distinguishing a PPII structure from a disordered structure is the presence of a positive peak around 220nm in the former but not in the latter. These spectra are now available for inclusion in new reference data sets used for CD analyses of the secondary structures of soluble proteins.