TAILIEUCHUNG - Báo cáo khoa học: The importance of being dimeric

Why are there so many dimeric proteins and enzymes? While for hetero-dimers a functional explanation seems quite reasonable, the case of homo-dimers is more puzzling. The number of homodimers found in all living organisms is rapidly increasing. A thorough inspection of the structural data from the available literature and stability (measured from denatura-tion–renaturation experiments) | iFEBS Journal REVIEW ARTICLE The importance of being dimeric Giampiero Mei1 2 Almerinda Di Venere1 2 Nicola Rosato1 2 and Alessandro Finazzi-Agro1 1 Department of ExperimentalMedicine and BiochemicalSciences University of Rome Tor Vergata Rome Italy 2 INFM University of Rome Tor Vergata Rome Italy Correspondence A. Finazzi-Agro Department of Experimental Medicine and Biochemical Sciences University of Rome Tor Vergata Via Montpellier 1 Rome 00133 Italy Fax 39 06 72596468 Tel 39 06 72596460 E-mail mei@ Note This paper is dedicated to the late G. Weber and . Blumberg who first stimulated our attention to the problem. Why are there so many dimeric proteins and enzymes While for heterodimers a functional explanation seems quite reasonable the case of homodimers is more puzzling. The number of homodimers found in all living organisms is rapidly increasing. A thorough inspection of the structural data from the available literature and stability measured from denatura-tion-renaturation experiments allows one to suggest that homodimers can be divided into three main types according to their mass and the presence of a relatively stable monomeric intermediate in the folding-unfolding pathway. Among other explanations we propose that an essential advantage for a protein being dimeric may be the proper and rapid assembly in the cellular milieu. Received 14 August 2004 revised 17 September 2004 accepted 21 September 2004 doi Introduction The world of globular proteins appears to a naive observer to be very complex. At first sight it is even difficult to find any regularities that may exist. In particular the ability of these macromolecules to reach their final shape among the many different conformations in a very short time is astonishing. Small globular proteins usually show some interesting correlations between their structural features and the thermodynamic parameters characterizing their overall stability 1 . Other .

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