Karthik Ramanna Livres

"Prudent, verifiable, and timely corporate accounting is a bedrock of our modern capitalist system. In recent years, however, the rules that govern corporate accounting have been subtly changed in ways that compromise these core principles, to the detriment of the economy at large. These changes have been driven by the private agendas of certain corporate special interests, aided selectively - and sometimes unwittingly - by arguments from business academia. With 'Political Standards, ' Karthik Ramanna develops the notion of 'thin political markets' to describe a key problem facing technical rule-making in corporate accounting. When standard-setting boards attempt to regulate the accounting practices of corporations, they must draw on a small pool of qualified experts - but those experts almost always have strong commercial interests in the outcome. Meanwhile, standard setting rarely enjoys much attention from the general public. This absence of accountability, Ramanna argues, allows corporate managers to game the system. In the profit-maximization framework of modern capitalism, the only practicable solution is to reframe managerial norms when participating in thin political markets. 'Political Standards' will be an essential resource for understanding how the rules of the game are set, whom they inevitably favor, and how the process can be changed for a better capitalism"--Jacket

Exploring the widespread outrage affecting organizations globally, this book provides insights into its causes and implications. It offers practical strategies for leaders to effectively address and manage this phenomenon, fostering resilience and positive change within their teams. By examining real-world examples, it highlights the importance of understanding employee sentiments and navigating the complexities of modern workplace dynamics. This unique perspective aims to equip leaders with the tools necessary for cultivating a more harmonious organizational environment.

This Brief reports on the interplay of an amino-acid mutation towards substrate which could lead to enhanced effects on mutant. These effects need  to  be given consideration in  the  engineering  processes of protein stability and further exploration of such learning are required to provide novel indication for selection of an enzymes.  There  are  very  few  reports  showing  such  stable,  energy  efficient  model  towards  improved  protein function prediction screening in-silico structure based mutagenesis of xylanases from Thermomyces lanuginosus​