Crystallisation of iPB-1 based on preserved helix conformation

SF was incompatible with PEG in some extent, and the phase separation took place in their blend film. The conformation of SF in the interface between SF and PEG was changed to the β-sheet, while that in the protein-rich domain remained in the random coil and/or helix conformation.

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Raman and normal-mode studies of the extended-helix conformation in polypeptide chains

Biopolymers ◽

10.1002/bip.360260011 ◽

1987 ◽

Vol 26 (S0) ◽

pp. S99-S107 ◽

Cited By ~ 10

Author(s):

P. K. Sengupta ◽

S. Krimm

Keyword(s):

Normal Mode ◽

Helix Conformation ◽

Polypeptide Chains

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Triple helix conformation-specific blinking of Cy3 in DNA

Chemical Communications ◽

10.1039/c5cc00607d ◽

2015 ◽

Vol 51 (23) ◽

pp. 4861-4864 ◽

Cited By ~ 8

Author(s):

Kiyohiko Kawai ◽

Atsushi Maruyama

Keyword(s):

Triple Helix ◽

Helix Conformation

We report that Cy3 undergoes triple helix conformation-specific blinking in DNA.

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Triple-Helix Conformation of a Polysaccharide Determined with Light Scattering, AFM, and Molecular Dynamics Simulation

Macromolecules ◽

10.1021/acs.macromol.8b02017 ◽

2018 ◽

Vol 51 (24) ◽

pp. 10150-10159 ◽

Cited By ~ 8

Author(s):

Yan Meng ◽

Xiaodan Shi ◽

Liqin Cai ◽

Shihai Zhang ◽

Kan Ding ◽

...

Keyword(s):

Molecular Dynamics ◽

Light Scattering ◽

Molecular Dynamics Simulation ◽

Triple Helix ◽

Dynamics Simulation ◽

Helix Conformation

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Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits

Brazilian Journal of Plant Physiology ◽

10.1590/s1677-04202003000200008 ◽

2003 ◽

Vol 15 (2) ◽

pp. 119-122 ◽

Cited By ~ 2

Author(s):

Marli Lourdes de Oliveira ◽

Leila Maria Beltramini ◽

Salvatore Giovanni de Simone ◽

Maria Helena Nasser Brumano ◽

Rosemeire Aparecida Silva-Lucca ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Terminal Amino Acid ◽

Saline Extract ◽

Hydrophobic Residues ◽

Terminal Amino ◽

Helix Conformation ◽

Far Ultraviolet ◽

Terminal Amino Acid Sequence

A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).

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