scholarly journals Conformational analysis of myotoxin alpha (muscle degenerating toxin) of Prairie rattlesnake venom. Predictions from amino acid sequence, circular dichroism, and Raman spectroscopy.

1979 ◽  
Vol 254 (18) ◽  
pp. 8922-8926
Author(s):  
G.S. Bailey ◽  
J. Lee ◽  
A.T. Tu
Keyword(s):  
Raman Spectroscopy ◽  
Circular Dichroism ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Conformational Analysis ◽  
Rattlesnake Venom ◽  
Circular Dichroïsm

Conformational analysis of thymidylate synthase from amino acid sequence and circular dichroism

Biochemistry ◽  
1986 ◽  
Vol 25 (21) ◽  
pp. 6650-6655 ◽  
Author(s):  
Parthasarathy Manavalan ◽  
Denice M. Mittelstaedt ◽  
Michael I. Schimerlik ◽  
W. Curtis Johnson
Keyword(s):  
Circular Dichroism ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Conformational Analysis ◽  
Thymidylate Synthase ◽  
Circular Dichroïsm

Circular dichroism studies of sheep β-lipotropic hormone

1976 ◽  
Vol 54 (11) ◽  
pp. 992-998 ◽  
Author(s):  
Serge St-Pierre ◽  
Claude Gilardeau ◽  
Michel Chrétien
Keyword(s):  
Circular Dichroism ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Conformational Transition ◽  
Acidic Solutions ◽  
Nacl Concentration ◽  
Helical Content ◽  
The Stability ◽  
Far Ultraviolet ◽  
Circular Dichroïsm

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.

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
Keyword(s):  
Circular Dichroism ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Secondary Structures ◽  
X Ray ◽  
Circular Dichroïsm ◽  
Human Prealbumin
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