Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins

1994 ◽  
Vol 23 (4) ◽  
pp. 253-262 ◽  
Author(s):  
RobertW. Woody
Keyword(s):  
Circular Dichroism ◽  
Side Chains ◽  
Far Ultraviolet ◽  
Circular Dichroïsm ◽  
Tryptophan Side Chains

Circular dichroism of cyclic hexapeptides with one and two side chains

Biochemistry ◽  
1971 ◽  
Vol 10 (8) ◽  
pp. 1330-1335 ◽  
Author(s):  
C. Allen Bush ◽  
Stanley M. Ziegler
Keyword(s):  
Circular Dichroism ◽  
Side Chains ◽  
Cyclic Hexapeptides ◽  
Circular Dichroïsm

Stabilizing Interactions between Aromatic and Basic Side Chains in α-Helical Peptides and Proteins. Tyrosine Effects on Helix Circular Dichroism

2002 ◽  
Vol 124 (43) ◽  
pp. 12706-12714 ◽  
Author(s):  
Charles D. Andrew ◽  
Samita Bhattacharjee ◽  
Nicoleta Kokkoni ◽  
Jonathan D. Hirst ◽  
Gareth R. Jones ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Side Chains ◽  
Helical Peptides ◽  
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.

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