Examining the secondary structures of unnatural peptides and carbohydrate-based compounds utilizing circular dichroism

2000 ◽  
Vol 11 (2) ◽  
pp. 337-362 ◽  
Author(s):  
Katherine D McReynolds ◽  
Jacquelyn Gervay-Hague
Keyword(s):  
Circular Dichroism ◽  
Secondary Structures ◽  
Unnatural Peptides ◽  
Circular Dichroïsm

scholarly journals Theoretical study of two-photon circular dichroism on molecular structures simulating aromatic amino acid residues in proteins with secondary structures

RSC Advances ◽  
2014 ◽  
Vol 4 (105) ◽  
pp. 60974-60986 ◽  
Author(s):  
Yuly Vesga ◽  
Carlos Diaz ◽  
Florencio E. Hernandez
Keyword(s):  
Circular Dichroism ◽  
Comparative Analysis ◽  
Theoretical Study ◽  
Secondary Structures ◽  
Molecular Structures ◽  
Random Coil ◽  
Amino Acid Residues ◽  
Two Photon ◽  
Α Helix ◽  
Circular Dichroïsm

Calculation and comparative analysis of the theoretical two-photon circular dichroism (TPCD) spectra of l-His, l-Phe, and l-Tyr simulating residues in proteins with secondary structures (α-helix, β-strand and random coil), down to the far-UV region (FUV).

Remarkably high solvatochromism in the circular dichroism spectra of the polyproline-II conformation: limitations or new opportunities?

2021 ◽  
Author(s):  
Vladimir Kubyshkin ◽  
Jochen Bürck ◽  
Oleg Babii ◽  
Nediljko Budisa ◽  
Anne S. Ulrich
Keyword(s):  
Circular Dichroism ◽  
Conventional Method ◽  
Secondary Structures ◽  
Circular Dichroism Spectra ◽  
Polyproline Ii ◽  
Circular Dichroïsm

Circular dichroism is a conventional method for studying the secondary structures of peptides and proteins and their transitions. While certain circular dichroism features are characteristic of α-helices and β-strands, the...

scholarly journals The E1→E2 transition of Ca2+-transporting ATPase in sarcoplasmic reticulum occurs without major changes in secondary structure. A circular-dichroism study

1987 ◽  
Vol 241 (3) ◽  
pp. 663-669 ◽  
Author(s):  
P Csermely ◽  
C Katopis ◽  
B A Wallace ◽  
A Martonosi
Keyword(s):  
Circular Dichroism ◽  
Sarcoplasmic Reticulum ◽  
Secondary Structure ◽  
Fluorescein Isothiocyanate ◽  
Secondary Structures ◽  
Backbone Conformation ◽  
Polypeptide Backbone ◽  
Circular Dichroïsm

C.d. spectroscopy was used to investigate the structures of Ca2+-ATPase (Ca2+-transporting ATPase) in the E1 and E2 states in native, in fluorescein isothiocyanate (FITC)-labelled and in solubilized sarcoplasmic reticulum (SR) preparations. The E1 state was stabilized by 100 microM-Ca2+ and the E2 state by 0.5 mM-Na3 VO4 and 0.1 mM-EGTA. There were no significant differences detected in the c.d. spectra and the calculated secondary structures between the E1 and E2 states in any of the three types of preparations. The FITC-labelled SR did show the characteristic changes in FITC fluorescence on addition of Ca2+ or vanadate, indicating that the preparation was competent for E1----E2 transitions. Therefore the absence of changes in the c.d. spectra implies that the E1----E2 transition in the Ca2+-ATPase does not involve a major net rearrangement of the polypeptide backbone conformation.

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