scholarly journals A Simple Model of Protein Folding: From Crystal Structure to the Living Cell

2012 ◽  
Vol 102 (3) ◽  
pp. 210a
Author(s):  
Maxim B. Prigozhin ◽  
Sharlene Denos
1997 ◽  
Vol 36 (19) ◽  
pp. 4172-4181 ◽  
Author(s):  
Hideo Imoto ◽  
Hiroshi Fukuoka ◽  
Shigenori Tsunesawa ◽  
Hisaya Horiuchi ◽  
Takao Amemiya ◽  
...  

2015 ◽  
Vol 71 (9) ◽  
pp. 1189-1193 ◽  
Author(s):  
Yoshiki Aikawa ◽  
Hiroshi Kida ◽  
Yuichi Nishitani ◽  
Kunio Miki

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.


2002 ◽  
Vol 58 (4) ◽  
pp. 662-672 ◽  
Author(s):  
Claire Gervais ◽  
Gérard Coquerel

The basic principles of a model predicting new lattices from a known crystal structure are described. The first of the two-step procedure consists of extracting one- or two-dimensional periodic fragments (PF) from the mother structure. In the second step, symmetry operators are added to the PFs in order to generate one or several new three-dimensional lattices consistent with the 230 space groups. Most of the examples are related to polymorphism, but relationships between racemic compounds and enantiomers, twinning and lamellar epitaxy phenomena are also exemplified.


2011 ◽  
Vol 9 (13) ◽  
pp. 4802 ◽  
Author(s):  
Wei-Yong Liu ◽  
Hai-Ying Li ◽  
Bao-Xiang Zhao ◽  
Jun-Ying Miao

1992 ◽  
Vol 47 (8) ◽  
pp. 1185-1188 ◽  
Author(s):  
Wolfgang Hiller ◽  
Akira Nishinaga ◽  
Anton Rieker

Flavonolatocobalt(III)(salen), a model enzyme-substrate-complex for the quercetinase reaction, was synthesized and its crystal structure determined. C31H23CoN2O5 · 2 CH2Cl2, M = 732.35, triclinic, space group P 1̅ , a = 12.463(2), b = 13.270(2), c = 10.041(2) Å, α = 97.89(1)°, β= 108.08(1)°, γ= 83.56(1)°, U = 1559.4 Å3, Z = 2.


2011 ◽  
Vol 2 (4) ◽  
pp. 314-319 ◽  
Author(s):  
Simon Ebbinghaus ◽  
Martin Gruebele
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document