scholarly journals YidC Protein, a Molecular Chaperone for LacY Protein Folding via the SecYEG Protein Machinery

2013 ◽  
Vol 288 (39) ◽  
pp. 28180-28194 ◽  
Author(s):  
Lu Zhu ◽  
H. Ronald Kaback ◽  
Ross E. Dalbey
Keyword(s):  
Protein Folding ◽  
Molecular Chaperone ◽  
Protein A

Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1

1993 ◽  
Vol 339 (1289) ◽  
pp. 313-326 ◽  
Keyword(s):  
Protein Folding ◽  
Mechanism Of Action ◽  
Molecular Chaperone ◽  
Polypeptide Chain ◽  
Family Members ◽  
Chain Folding ◽  
Cell Functions ◽  
Cellular Compartments

Two families of molecular chaperone, the hsp 60-GroEL family and the TF55-TCP1 family, have been discovered in evolutionarily related cellular compartments. A member of one of these families, hsp 60, has been shown to play a global role in polypeptide chain folding in mitochondria. We review here studies of both hsp 60 and other family members, discussing their essential physiological roles and mechanism of action.

scholarly journals Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin fromHomo sapiens

2015 ◽  
Vol 71 (9) ◽  
pp. 1189-1193 ◽  
Author(s):  
Yoshiki Aikawa ◽  
Hiroshi Kida ◽  
Yuichi Nishitani ◽  
Kunio Miki
Keyword(s):  
Crystal Structure ◽  
Protein Folding ◽  
Diffraction Data ◽  
Molecular Chaperone ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Native Proteins ◽  
Group Ii Chaperonin

Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non-native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non-native actin and tubulin to chaperonin-containing TCP-1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space groupP21212, with unit-cell parametersa= 123.2,b= 152.4,c= 105.9 Å.

scholarly journals Kinks, loops, and protein folding, with protein A as an example

2014 ◽  
Vol 140 (2) ◽  
pp. 025101 ◽  
Author(s):  
Andrey Krokhotin ◽  
Adam Liwo ◽  
Gia G. Maisuradze ◽  
Antti J. Niemi ◽  
Harold A. Scheraga
Keyword(s):  
Protein Folding ◽  
Protein A

Phage Tailspike Protein: A fishy tale of protein folding

1994 ◽  
Vol 4 (11) ◽  
pp. 1026-1029 ◽  
Author(s):  
D.P. Goldenberg ◽  
T.E. Creighton
Keyword(s):  
Protein Folding ◽  
Protein A ◽  
Tailspike Protein

scholarly journals Calcium-mediated Protein Folding and Stabilization of Salmonella Biofilm-associated Protein A

2019 ◽  
Vol 431 (2) ◽  
pp. 433-443 ◽  
Author(s):  
Durgarao Guttula ◽  
Mingxi Yao ◽  
Karen Baker ◽  
Liang Yang ◽  
Benjamin T. Goult ◽  
...  
Keyword(s):  
Protein Folding ◽  
Protein A
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