Journal ArticleDOI
Protein folding in the cell.
TLDR
Folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.Abstract:
In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the absence of other macromolecular cellular components, folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.read more
Citations
More filters
Journal ArticleDOI
Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
TL;DR: This work discloses that expression of Hsps can occur in nature, all species have hsp genes but they vary in the patterns of their expression, and Hsp expression can be correlated with resistance to stress, and species' thresholds for HSP expression are correlated with levels of stress that they naturally undergo.
Journal ArticleDOI
Molecular chaperones in cellular protein folding.
TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
Journal ArticleDOI
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
TL;DR: Understanding how the thousands of different proteins synthesized in a cell use this chaperone machinery has profound implications for biotechnology and medicine.
Journal ArticleDOI
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
TL;DR: The cloning of perk is described, a gene encoding a type I transmembrane ER-resident protein that contains a protein-kinase domain most similar to that of the known eIF2α kinases, PKR and HRI that implicate PERK in a signalling pathway that attenuates protein translation in response to ER stress.
Journal ArticleDOI
The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins
D A Parsell,Susan Lindquist +1 more
TL;DR: The Lon Protease, DnaK.T URNOVER of AB ERR ANT PROT EINS in E. COLI, and more.
References
More filters
Journal ArticleDOI
The Protein Data Bank: a computer-based archival file for macromolecular structures.
Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
TL;DR: The Protein Data Bank is a computer-based archival file for macromolecular structures that stores in a uniform format atomic co-ordinates and partial bond connectivities, as derived from crystallographic studies.
Journal ArticleDOI
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
Journal ArticleDOI
The heat-shock response
TL;DR: A comparison of different Organisms and Stages of Development and Heat-Induced Lethality and Thermotolerance and the role of RNA Processing are presented.
Journal ArticleDOI
Structure of the human class I histocompatibility antigen, HLA-A2.
Pamela J. Bjorkman,Mark A. Saper,Boudjéma Samraoui,W. S. Bennett,W. S. Bennett,Jack L. Strominger,Don C. Wiley +6 more
TL;DR: The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner and the region distal from the membrane is a platform of eight antiparallel β-strands topped by α-helices.
Journal ArticleDOI
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution.
TL;DR: The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded coiled-coil of α-helices extends 76 Å from the membrane and a globular region of antiparallel β-sheet is positioned on top of this stem.