Molecular chaperones in cellular protein folding

Bioessays 16 (9):689-692 (1994)
  Copy   BIBTEX

Abstract

The discovery of “molecular chaperones” has dramatically changed our concept of cellular protein folding. Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformation in a reaction mediated by these versatile helper proteins. Understanding the structure and function of molecular chaperones is likely to yield useful applications for medicine and biotechnology in the future.

Links

PhilArchive



    Upload a copy of this work     Papers currently archived: 91,386

External links

Setup an account with your affiliations in order to access resources via your University's proxy server

Through your library

Similar books and articles

Proteins, the chaperone function and heredity.Valeria Mosini - 2013 - Biology and Philosophy 28 (1):53-74.
The Protein Side of the Central Dogma: Permanence and Change.Michel Morange - 2006 - History and Philosophy of the Life Sciences 28 (4):513 - 524.
Molecular Epigenesis, Molecular Pleiotropy, and Molecular Gene Definitions.Richard Burian - 2004 - History and Philosophy of the Life Sciences 26 (1):59 - 80.
Molecular Biology and Pauling's Immunochemistry: A Neglected Dimension.Lily E. Kay - 1989 - History and Philosophy of the Life Sciences 11 (2):211 - 219.

Analytics

Added to PP
2013-11-23

Downloads
13 (#1,010,467)

6 months
5 (#629,136)

Historical graph of downloads
How can I increase my downloads?