scholarly journals Application of Circular Dichroism and Fluorescence Spectroscopies To Assess Photostability of Water-Soluble Porcine Lens Proteins

ACS Omega ◽  
2020 ◽  
Vol 5 (8) ◽  
pp. 4293-4301 ◽  
Author(s):  
Claudia Honisch ◽  
Viola Donadello ◽  
Rohanah Hussain ◽  
Daniele Peterle ◽  
Vincenzo De Filippis ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Water Soluble ◽  
Lens Proteins ◽  
Circular Dichroïsm

Water-soluble lysine-containing polypeptides. IV. The synthesis, characterization,and circular dichroism spectra of sequential polypeptides formed from dipeptides of lysine and amino acids of increasing side chain size

1977 ◽  
Vol 55 (24) ◽  
pp. 4257-4266 ◽  
Author(s):  
Lewis A. Slotin ◽  
Denis R. Lauren ◽  
Ross E. Williams
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Gel Filtration ◽  
Circular Dichroism Spectroscopy ◽  
Water Soluble ◽  
Side Chain ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm

Several polypeptides have been synthesized which contain the alternating sequence lysyl-X, where X = gly, L-ala, D-ala, L-val, L-leu, and L-phe. The polypeptides have been characterized by gel filtration (molecular weight) and by circular dichroism spectroscopy (secondary structure).

scholarly journals UV-CD12: synchrotron radiation circular dichroism beamline at ANKA

2015 ◽  
Vol 22 (3) ◽  
pp. 844-852 ◽  
Author(s):  
Jochen Bürck ◽  
Siegmar Roth ◽  
Dirk Windisch ◽  
Parvesh Wadhwani ◽  
David Moss ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Lipid Bilayers ◽  
Spectral Range ◽  
Signal To Noise Ratio ◽  
Linear Dichroism ◽  
Water Soluble ◽  
Protein Films ◽  
Hydrated Protein ◽  
Circular Dichroïsm

Synchrotron radiation circular dichroism (SRCD) is a rapidly growing technique for structure analysis of proteins and other chiral biomaterials. UV-CD12 is a high-flux SRCD beamline installed at the ANKA synchrotron, to which it had been transferred after the closure of the SRS Daresbury. The beamline covers an extended vacuum-UV to near-UV spectral range and has been open for users since October 2011. The current end-station allows for temperature-controlled steady-state SRCD spectroscopy, including routine automated thermal scans of microlitre volumes of water-soluble proteins down to 170 nm. It offers an excellent signal-to-noise ratio over the whole accessible spectral range. The technique of oriented circular dichroism (OCD) was recently implemented for determining the membrane alignment of α-helical peptides and proteins in macroscopically oriented lipid bilayers as mimics of cellular membranes. It offers improved spectral quality <200 nm compared with an OCD setup adapted to a bench-top instrument, and accelerated data collection by a factor of ∼3. In addition, it permits investigations of low hydrated protein films down to 130 nm using a rotatable sample cell that avoids linear dichroism artifacts.

Alpha and beta conformations of water soluble sequential iso polypeptides

1988 ◽  
Vol 53 (11) ◽  
pp. 2825-2832 ◽  
Author(s):  
Bernard Barbier ◽  
Margarita Perello ◽  
André Brack
Keyword(s):  
Circular Dichroism ◽  
Water Soluble ◽  
Helical Conformation ◽  
Molecular Weights ◽  
Helix Formation ◽  
Α Helix ◽  
Circular Dichroïsm ◽  
Β Sheet ◽  
Protected Peptides

Alternating poly(Leu-Lys) and its isopolypeptide poly(Leu-Lys-Lys-Leu) were synthesized via polycondensation of p-nitrophenyl esters of the corresponding protected peptides. Addition of one equivalent of 1-hydroxybenzotriazole and varying amounts of a tertiary base allowed to control the molecular weights of the samples. The conformation of the water soluble polypeptides was investigated by circular dichroism. Poly(Leu-Lys) adopts a β-sheet conformation in the presence of salt while poly(Leu-Lys-Lys-Leu) adopts an α-helical conformation. For polypeptides based on a 1 : 1 composition of hydrophobic (A) and hydrophilic (B) residues, the shortest repeat for the formation of a β-sheet is -AB- whereas -AABB- represents the shortest repeat for an α-helix formation.

Water-soluble lysine-containing polypeptides. V. Circular dichroisrm, electron microscopic, and thermal denaturation studies of the interaction of poly(L-lysyl-L-alanine) and poly(L-lysyl-D-alanine) with calf thymus DNA

1978 ◽  
Vol 56 (20) ◽  
pp. 2650-2656 ◽  
Author(s):  
Sandra L. Kielland ◽  
Lewis A. Slotin ◽  
Ross E. Williams
Keyword(s):  
Circular Dichroism ◽  
Secondary Structure ◽  
Electron Micrographs ◽  
Thermal Denaturation ◽  
Water Soluble ◽  
Calf Thymus Dna ◽  
Circular Dichroism Spectra ◽  
Electron Microscopic ◽  
Calf Thymus ◽  
Circular Dichroïsm

Turbidity measurements, circular dichroism spectra, electron micrographs and thermal denaturation profiles of complexes between sonicated DNA and either poly(L-lysyl-L-alanine) or poly(L-lysyl-D-alanine) show significant differences which might be related to the primary or secondary structure of the polypeptides.

Sign in / Sign up

Export Citation Format

Share Document