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010   $a981-10-4651-4
024 7 $a10.1007/978-981-10-4651-3
035   $a(CKB)3710000001631555
035   $a(DE-He213)978-981-10-4651-3
035   $a(MiAaPQ)EBC4996360
035   $a(PPN)203848527
035   $a(EXLCZ)993710000001631555
100   $a20170830d2017      u|         0
101 0 $aeng
135   $aurnn#008mamaa
181   $ctxt$2rdacontent
182   $cc$2rdamedia
183   $acr$2rdacarrier
200 10$aProkaryotic Chaperonins $eMultiple Copies and Multitude Functions /$fedited by C. M. Santosh Kumar, Shekhar C. Mande
205   $a1st ed. 2017.
210  1$aSingapore :$cSpringer Singapore :$cImprint: Springer,$d2017.
215   $a1 online resource (IX, 170 p. 46 illus., 38 illus. in color.)
225 1 $aHeat Shock Proteins,$x1877-1246 ;$v11
311 08$a981-10-4650-6 
320   $aIncludes bibliographical references at the end of each chapters.
327   $aChapter 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.
330   $aThis book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology ? more specifically, in protein folding pathways. .
410  0$aHeat Shock Proteins,$x1877-1246 ;$v11
606   $aProteins
606   $aMicrobiology
606   $aBiophysics
606   $aBiophysics
606   $aBiomedical engineering
606   $aCell physiology
606   $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040
606   $aMicrobiology$3https://scigraph.springernature.com/ontologies/product-market-codes/L23004
606   $aBiological and Medical Physics, Biophysics$3https://scigraph.springernature.com/ontologies/product-market-codes/P27008
606   $aBiomedical Engineering/Biotechnology$3https://scigraph.springernature.com/ontologies/product-market-codes/B24000
606   $aCell Physiology$3https://scigraph.springernature.com/ontologies/product-market-codes/L33010
615  0$aProteins.
615  0$aMicrobiology.
615  0$aBiophysics.
615  0$aBiophysics.
615  0$aBiomedical engineering.
615  0$aCell physiology.
615 14$aProtein Science.
615 24$aMicrobiology.
615 24$aBiological and Medical Physics, Biophysics.
615 24$aBiomedical Engineering/Biotechnology.
615 24$aCell Physiology.
676   $a572.6
702   $aKumar$b C. M. Santosh$4edt$4http://id.loc.gov/vocabulary/relators/edt
702   $aMande$b Shekhar C.$4edt$4http://id.loc.gov/vocabulary/relators/edt
906   $aBOOK
912   $a9910253947603321
996   $aProkaryotic Chaperonins$92133982
997   $aUNINA