An Efficient Low Storage and Memory Treatment of Gridded Interaction Fields for Simulations of Macromolecular Association

2016 ◽  
Vol 12 (9) ◽  
pp. 4563-4577
Author(s):  
Musa Ozboyaci ◽  
Michael Martinez ◽  
Rebecca C. Wade
Keyword(s):  
Macromolecular Association

Gel Permeation Analysis of Macromolecular Association by an Equilibrium Method

1971 ◽  
Vol 6 (2) ◽  
pp. 217-228 ◽  
Author(s):  
Bruce F. Cameron ◽  
Larry Sklar ◽  
Veronika Greenfield ◽  
Alan D. Adler
Keyword(s):  
Equilibrium Method ◽  
Gel Permeation ◽  
Macromolecular Association

scholarly journals Rabbit muscle myogen. Interactions with phosphate as the source of non-enantiography in moving-boundary electrophoresis

1976 ◽  
Vol 157 (3) ◽  
pp. 699-704 ◽  
Author(s):  
S J Lovell ◽  
D J Winzor
Keyword(s):  
Phosphate Buffer ◽  
Moving Boundary ◽  
Potassium Phosphate ◽  
Glycolytic Enzymes ◽  
Velocity Sedimentation ◽  
Rabbit Muscle ◽  
Potassium Phosphate Buffer ◽  
Electrophoretic Patterns ◽  
Macromolecular Association

Rabbit muscle myogen has been subjected to moving-boundary electrophoresis and velocity sedimentation in 0.0187 M-potassium phosphate buffer, pH7.7, I = 0.05. The ascending and descending and descending electrophoretic patterns are sufficiently non-enantiographic to suggest the existence of rapid, reversible interactions in the myogen solutions. However, no evidence of pronounced macromolecular association was obtained in velocity-sedimentation experiments. The source of the non-enantiography in electrophoresis has been traced to interactions of phosphate with components of myogen, which should therefore be considered as a mixutre, rather than a complex, of glycolytic enzymes.

Influence of the pyruvate content of xanthan on macromolecular association in solution

1981 ◽  
Vol 3 (2) ◽  
pp. 129-134 ◽  
Author(s):  
I.H. Smith ◽  
K.C. Symes ◽  
C.J. Lawson ◽  
E.R. Morris
Keyword(s):  
Macromolecular Association
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