Dynamics of reversible supramolecular polymers: Independent determination of the dependence of linear viscoelasticity on concentration and chain length by using chain stoppers

2005 ◽  
Vol 7 (11) ◽  
pp. 2390 ◽  
Author(s):  
W. Knoben ◽  
N. A. M. Besseling ◽  
L. Bouteiller ◽  
M.A. Cohen Stuart
Keyword(s):  
Chain Length ◽  
Linear Viscoelasticity ◽  
Supramolecular Polymers ◽  
Independent Determination

scholarly journals Model-Independent Determination of the Spin of the Ω− and Its Polarization Alignment in ψ(3686)→Ω−Ω¯+

2021 ◽  
Vol 126 (9) ◽  
Author(s):  
M. Ablikim ◽  
M. N. Achasov ◽  
P. Adlarson ◽  
S. Ahmed ◽  
M. Albrecht ◽  
...  
Keyword(s):  
Independent Determination ◽  
Model Independent

Orthogonal chain length control in calix[5]arene-based AB-type supramolecular polymers

2011 ◽  
Vol 52 (48) ◽  
pp. 6460-6464 ◽  
Author(s):  
Claudia Gargiulli ◽  
Giuseppe Gattuso ◽  
Anna Notti ◽  
Sebastiano Pappalardo ◽  
Melchiorre F. Parisi
Keyword(s):  
Chain Length ◽  
Supramolecular Polymers

scholarly journals A METHOD FOR THE INDEPENDENT DETERMINATION OF CYSTEINE AND CYSTINE IN PROTEINS

1954 ◽  
Vol 207 (2) ◽  
pp. 903-910
Author(s):  
R.D. Strickland ◽  
E.L. Martin ◽  
J.L. Riebsomer
Keyword(s):  
Independent Determination

Mean Chain Length of Adsorbed Supramolecular Polymers

2006 ◽  
Vol 96 (7) ◽  
Author(s):  
Henk J. A. Zweistra ◽  
N. A. M. Besseling
Keyword(s):  
Chain Length ◽  
Supramolecular Polymers

On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase

1981 ◽  
Vol 293 (1063) ◽  
pp. 159-171 ◽  
Keyword(s):  
Catalytic Mechanism ◽  
Polypeptide Chain ◽  
Three Dimensional ◽  
Triose Phosphate Isomerase ◽  
Dimensional Structure ◽  
Dihydroxyacetone Phosphate ◽  
Triose Phosphate ◽  
Independent Determination ◽  
Chicken Muscle

Triose phosphate isomerase is a dimeric enzyme of molecular mass 56000 which catalyses the interconversion of dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate. The crystal structure of the enzyme from chicken muscle has been determined at a resolution of 2.5 A, and an independent determination of the structure of the yeast enzyme has just been completed at 3 A resolution. The conformation of the polypeptide chain is essentially identical in the two structures, and consists of an inner cylinder of eight strands of parallel |3-pleated sheet, with mostly helical segments connecting each strand. The active site is a pocket containing glutamic acid 165, which is believed to act as a base in the reaction. Crystallographic studies of the binding of DHAP to both the chicken and the yeast enzymes reveal a common mode of binding and suggest a mechanism for catalysis involving polarization of the substrate carbonyl group.

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