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In particular, the initiation of eukaryotic protein synthesis requires roughly an order of magnitude more initiation factors to promote efficient mRNA recruitment and ribosomal recognition of the start codon than are needed for eubacterial initiation. The mechanisms by which these initiation factors promote ribosome conformational changes during stages of initiation have been studied using cross-linking, footprinting, site-directed probing, cryo-electron microscopy, X-ray crystallography, fluorescence spectroscopy and single-molecule techniques. Here, we review how the results of these different approaches have begun to converge to yield a detailed molecular understanding of the dynamic motions that the eukaryotic ribosome cycles through during the initiation of protein synthesis.<\/jats:p>","DOI":"10.1017\/s0033583507004647","type":"journal-article","created":{"date-parts":[[2007,12,12]],"date-time":"2007-12-12T11:26:54Z","timestamp":1197458814000},"page":"163-189","source":"Crossref","is-referenced-by-count":8,"title":["Quantitative studies of ribosome conformational dynamics"],"prefix":"10.1017","volume":"40","author":[{"given":"Christopher S.","family":"Fraser","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jennifer 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