Water-soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine-Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

1975 ◽  
Vol 53 (14) ◽  
pp. 2210-2210
Author(s):  
Ross E. Williams ◽  
Sandra L. Kielland
Keyword(s):  
Circular Dichroism ◽  
Water Soluble ◽  
Dna Conformation ◽  
Circular Dichroïsm

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Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

1975 ◽  
Vol 53 (4) ◽  
pp. 542-548 ◽  
Author(s):  
Ross E. Williams ◽  
Sandra L. Kielland
Keyword(s):  
Circular Dichroism ◽  
Nucleic Acid ◽  
Water Soluble ◽  
Dna Conformation ◽  
Protein Nucleic Acid ◽  
Circular Dichroïsm ◽  
Circular Dichroic

To serve as models of protein–nucleic acid complexes, annealed complexes of several sequential lysine–glycine polypeptides with DNA have been formed. Circular dichroic spectra of the DNA contained in the complexes indicates that several discrete conformations of DNA can exist when complexed.

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.

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

The Left-Handed Z-DNA Conformation in Oligodeoxynucleotides Containing Different Amounts of AT Base Pairs: A Far UV Circular Dichroism Study

1989 ◽  
Vol 6 (6) ◽  
pp. 1217-1231 ◽  
Author(s):  
Luigi Emilio Xodo ◽  
Giorgio Manzini ◽  
Franco Quadrifoglio ◽  
Narayanarao Yathindra ◽  
Gijs A. van der Marel ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Dna Conformation ◽  
Base Pairs ◽  
Left Handed ◽  
Z Dna ◽  
Circular Dichroïsm
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