Comparison of X-ray data to estimated secondary structures from amino acid sequence and circular dichroism of human prealbumin

1976 ◽  
Vol 73 ◽  
pp. 1018-1023 ◽  
Author(s):  
Jean Garnier ◽  
Roland Salesse ◽  
Berthe Rérat ◽  
Claude Rérat ◽  
Colin Blake
Biochemistry ◽  
1986 ◽  
Vol 25 (21) ◽  
pp. 6650-6655 ◽  
Author(s):  
Parthasarathy Manavalan ◽  
Denice M. Mittelstaedt ◽  
Michael I. Schimerlik ◽  
W. Curtis Johnson

1976 ◽  
Vol 54 (11) ◽  
pp. 992-998 ◽  
Author(s):  
Serge St-Pierre ◽  
Claude Gilardeau ◽  
Michel Chrétien

The far ultraviolet circular dichroism spectra of sheep β-lipotropic hormone (β-LPH) were recorded under different conditions of pH, temperature, salt concentration, and solvent composition. Results confirm the stability of the hormone in strong basic or acidic solutions; moreover, temperatures up to 50 °C do not seem to affect noticeably the conformation of β-LPH. However, increasing the NaCl concentration or addition of dioxane in the solution brings about a conformational transition of the chain, interpreted as an increase in the helical content. The method of Yang (Chen, Y. H., Yang, J. T. &Martinez, H. M. (1972) Biochemistry 11, 4120–4131) was used to compute the proportion of helical, β, and unordered forms of the hormone chain. The proportions are compared with those obtained from Fasman's predictive method (Chou, P. Y. &Fasman, G. D. (1974) Biochemistry 13, 211–221 and Chou, P. Y. &Fasman, G. D. (1974) Biochemistry 13, 222–245) based on the known amino acid sequence of β-LPH.


2005 ◽  
Vol 144-147 ◽  
pp. 271-273 ◽  
Author(s):  
K. Nakagawa ◽  
F. Kaneko ◽  
Y. Ohta ◽  
M. Tanaka ◽  
T. Kitada ◽  
...  

2020 ◽  
Vol 116 (20) ◽  
pp. 201905
Author(s):  
Biqiong Yu ◽  
Guichuan Yu ◽  
Jeff Walter ◽  
Vipul Chaturvedi ◽  
Joseph Gotchnik ◽  
...  

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