| Range |
Length 80 to 100: Width ~10 to 20 Å
|
| Organism |
Archaea Haloarcula marismortui |
| Reference |
Zhang G, Ignatova Z. Folding at the birth of the nascent chain: coordinating translation with co-translational folding. Curr Opin Struct Biol. 2011 Feb21(1):25-31. doi: 10.1016/j.sbi.2010.10.008. p.27 left column 2nd paragraphPubMed ID21111607
|
| Primary Source |
Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science. 2000 Aug 11 289(5481):905-20.PubMed ID10937989
|
| Method |
(Primary source abstract:) "[Researchers] determined the crystal structure of the large ribosomal subunit from Haloarcula marismortui at 2.4 angstrom resolution." |
| Comments |
P.27 left column 2nd paragraph: "The first environment a newly synthesized peptide encounters is the ribosomal exit tunnel which resembles a tube 80–100 Å in length and ~10–20 Å in width [primary source]. The ribosomal tunnel is not a passive receptacle for nascent chains and may play an active role in inducing
and/or stabilizing compact structures." See Kudva et al., 2013 PMID 23567322 P.511 right column bottom paragraph: "Proteins are synthesised at a rate of 10-20 amino acids per second (BNID 113762), the ribosomal tunnel has a length of approx. 100 Å (Nissen et al., 2000) and a single amino acid occupies approx. 3.5 Å." |
| Entered by |
Uri M |
| ID |
109578 |