The first of its kind, this volume presents the latest research findings on the chaperonins, the best studied family of a class of proteins known as molecular chaperones. These findings are changing our view of some fundamental cellular processes involving proteins, especially how proteins fold into their functional conformations. - Origins of the new view of protein folding - Prokaryotic chaperonins - Eukaryotic chaperonins - Evolution of the chaperonins - Refolding of denatured proteins - Organelle biosynthesis - Biomedical aspects

Soon to be a feature film from the creators of Downton Abbey starring Elizabeth McGovern, The Chaperone is a New York Times-bestselling novel about the woman who chaperoned an irreverent Louise Brooks to New York City in the 1920s and the summer that would change them both. Only a few years before becoming a famous silent-film star and an icon of her generation, a fifteen-year-old Louise Brooks leaves Wichita, Kansas, to study with the prestigious Denishawn School of Dancing in New York. Much to her annoyance, she is accompanied by a thirty-six-year-old chaperone, who is neither mother nor friend. Cora Carlisle, a complicated but traditional woman with her own reasons for making the trip, has no idea what she’s in for. Young Louise, already stunningly beautiful and sporting her famous black bob with blunt bangs, is known for her arrogance and her lack of respect for convention. Ultimately, the five weeks they spend together will transform their lives forever. For Cora, the city holds the promise of discovery that might answer the question at the core of her being, and even as she does her best to watch over Louise in this strange and bustling place she embarks on a mission of her own. And while what she finds isn’t what she anticipated, she is liberated in a way she could not have imagined. Over the course of Cora’s relationship with Louise, her eyes are opened to the promise of the twentieth century and a new understanding of the possibilities for being fully alive. Drawing on the rich history of the 1920s, ’30s, and beyond—from the orphan trains to Prohibition, flappers, and the onset of the Great Depression to the burgeoning movement for equal rights and new opportunities for women—Laura Moriarty’s The Chaperone illustrates how rapidly everything, from fashion and hemlines to values and attitudes, was changing at this time and what a vast difference it all made for Louise Brooks, Cora Carlisle, and others like them.

The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct folding and transport. This Guidebook catalogues the latest information on nearly 200 of these molecules, including the important class of heat shock proteins; each entry is written by leading researchers in the field.

Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology – more specifically, in protein folding pathways.

This book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?

Type I chaperonins are key players in maintaining the proteome of bacteria and organelles of bacterial origin. They are well known for their crucial role in mediating protein folding. For almost three decades, the molecular mechanism of chaperonin function has been the subject of intensive research. Still, surprising new mechanistic discoveries are constantly reported. It seems that we are far from having a full understanding of the chaperonin mode of action. Chaperonins are not simply protein folding machines. They also perform diverse extramitochondrial tasks, mainly related to inflammatory and signal transduction processes. This eBook constitutes ten articles highlighting the latest developments related to the divers functions of Type I chaperonins. As its title, mechanism and beyond, the collection starts with mechanistic view, continues with extracellular functions and ends with biotechnological applications of Type I chaperonins.

In this unique overview of the Hsp60 chaperonin, Peter Bross addresses molecular biologists, medical research scientists and individuals interested in molecular or general biology. First, Bross discusses the basics of the Hsp60 chaperonin in terms of its structure and the molecular mechanisms determining its function. Second, the author highlights the multiple roles of Hsp60 for cellular systems and regulatory pathways, especially in connection with neurodegenerative diseases caused by Hsp60 deficiency. Finally, the author highlights controversial observations suggesting additional, non-standard functions of Hsp60 in and outside mitochondria as well as possible gaps in our understanding of the chaperonin. This volume serves as a snapshot suitable for experienced researcher working in fields related to molecular chaperones yet still accessible to researchers entering the field.