Skip to main content

Tethering Creates Unusual Kinetics for Ribosome-Associated Chaperones with Nascent Chains

Buy Article:

$63.00 plus tax (Refund Policy)

Abstract:

This article focuses on ribosome-associated chaperones. A chaperone bound close to the exit tunnel on a ribosome 25 Å from the emerging nascent chain has an effective concentration of 1 x 10-1 M, which is 4-5 orders of magnitude larger than the concentration of the chaperone in the cytosol. Ribosome-bound chaperones bind nascent chains intramolecularly with rates as large as 104 s-1 in order to keep chains unfolded.





Keywords: Chaperone; holdase; kinetic partitioning; proximity effect; ribosome-associated chaperone

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986609788490195

Publication date: June 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2009/00000016/00000006/art00009
dcterms_title,dcterms_description,pub_keyword
6
5
20
40
5

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more