Prokaryotic Chaperonins Multiple Copies and Multitude Functions /

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 a...

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Λεπτομέρειες βιβλιογραφικής εγγραφής
Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
Άλλοι συγγραφείς: Kumar, C. M. Santosh (Επιμελητής έκδοσης), Mande, Shekhar C. (Επιμελητής έκδοσης)
Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
Γλώσσα:English
Έκδοση: Singapore : Springer Singapore : Imprint: Springer, 2017.
Σειρά:Heat Shock Proteins, 11
Θέματα:
Διαθέσιμο Online:Full Text via HEAL-Link
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245 1 0 |a Prokaryotic Chaperonins  |h [electronic resource] :  |b Multiple Copies and Multitude Functions /  |c edited by C. M. Santosh Kumar, Shekhar C. Mande. 
264 1 |a Singapore :  |b Springer Singapore :  |b Imprint: Springer,  |c 2017. 
300 |a IX, 170 p. 46 illus., 38 illus. in color.  |b online resource. 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
347 |a text file  |b PDF  |2 rda 
490 1 |a Heat Shock Proteins,  |x 1877-1246 ;  |v 11 
505 0 |a Chapter 1. Protein folding in the cell – the role of molecular chaperones -- Chapter 2. Structure and function of the Hsp60 Chaperonins -- Chapter 3. Classical View on the Regulation of Heat-shock response -- Chapter 4. Recent Advances in the Regulation of Heat-shock Response- Chapter 5. Multiple Chaperonins in Bacteria -- Chapter 6. Multiple Chaperonins in Mycobacteria -- Chapter 7. Dynamic interplay of the Myxobacterial chaperonins -- Chapter 8. Division of Labour in Rhizobial Chaperonins -- Chapter 9. Cooperativity of archaeal and bacterial chaperonins -- Chapter 10. Evolution of multiple chaperonins. 
520 |a 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. . 
650 0 |a Life sciences. 
650 0 |a Biomedical engineering. 
650 0 |a Proteins. 
650 0 |a Cell physiology. 
650 0 |a Microbiology. 
650 1 4 |a Life Sciences. 
650 2 4 |a Protein Science. 
650 2 4 |a Microbiology. 
650 2 4 |a Biological and Medical Physics, Biophysics. 
650 2 4 |a Biomedical Engineering/Biotechnology. 
650 2 4 |a Cell Physiology. 
700 1 |a Kumar, C. M. Santosh.  |e editor. 
700 1 |a Mande, Shekhar C.  |e editor. 
710 2 |a SpringerLink (Online service) 
773 0 |t Springer eBooks 
776 0 8 |i Printed edition:  |z 9789811046506 
830 0 |a Heat Shock Proteins,  |x 1877-1246 ;  |v 11 
856 4 0 |u http://dx.doi.org/10.1007/978-981-10-4651-3  |z Full Text via HEAL-Link 
912 |a ZDB-2-SBL 
950 |a Biomedical and Life Sciences (Springer-11642)