Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation:  Elucidation of the Molecular Mechanism†

Biochemistry ◽  
2001 ◽  
Vol 40 (20) ◽  
pp. 6036-6046 ◽  
Author(s):  
Liza Nielsen ◽  
Ritu Khurana ◽  
Alisa Coats ◽  
Sven Frokjaer ◽  
Jens Brange ◽  
...  
Keyword(s):  
Environmental Factors ◽  
Molecular Mechanism ◽  
Fibril Formation ◽  
Kinetics Of

scholarly journals Effect of Association State and Conformational Stability on the Kinetics of Immunoglobulin Light Chain Amyloid Fibril Formation at Physiological pH

2002 ◽  
Vol 277 (15) ◽  
pp. 12657-12665 ◽  
Author(s):  
Pierre O. Souillac ◽  
Vladimir N. Uversky ◽  
Ian S. Millett ◽  
Ritu Khurana ◽  
Sebastian Doniach ◽  
...  
Keyword(s):  
Light Chain ◽  
Amyloid Fibril ◽  
Conformational Stability ◽  
Fibril Formation ◽  
Immunoglobulin Light Chain ◽  
Amyloid Fibril Formation ◽  
Kinetics Of ◽  
Association State

The Role of Intermolecular Forces in the Mechanism of High-Elastic Deformation. I. The Molecular Mechanism and an Equation for the Kinetics of High Elastic Deformation

1951 ◽  
Vol 24 (2) ◽  
pp. 336-343
Author(s):  
B. A. Dogadkin ◽  
G. M. Bartenev ◽  
M. M. Reznikovskii˘
Keyword(s):  
Molecular Structure ◽  
Molecular Mechanism ◽  
Elastic Deformation ◽  
Approximate Equation ◽  
Intermolecular Forces ◽  
Joint Application ◽  
Balanced Configurations ◽  
Kinetics Of ◽  
Constant Deformation

Abstract 1. The molecular mechanism of the relaxation of deformation of high-elastic polymers has been studied. 2. It is shown that the slow relaxation, which is typical of high-elastic polymers, may be best explained as a restoration process, which either partial or complete (depending on the degree of development of side chains in the molecular structure formed by the main valence chains) of the balanced configurations of the molecular chains. 3. It is shown that the rate of the relaxation process in this case is determined by the molecular activity of the particular polymer. 4. An approximate equation for the kinetics of high-elastic deformation which expresses qualitatively the mechanical properties of high-elastic polymers is proposed. 5. Hypotheses concerning the relation between the time of relaxation and the unbalanced stress are advanced. Equation (2) is derived as characteristic of this relation. 6. It is shown that the joint application of Equations (1) and (2) makes it possible to describe qualitatively the relaxation of stress at constant deformation.

Early Kinetics of Amyloid Fibril Formation Reveals Conformational Reorganisation of Initial Aggregates

2007 ◽  
Vol 366 (4) ◽  
pp. 1351-1363 ◽  
Author(s):  
N. Cerdà-Costa ◽  
A. Esteras-Chopo ◽  
F.X. Avilés ◽  
L. Serrano ◽  
V. Villegas
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Kinetics Of

The influence of environmental factors on the kinetics of a biosynthetic process

1973 ◽  
Vol 36 (3) ◽  
pp. 339-356 ◽  
Author(s):  
L. A. Muzychenko ◽  
V. M. Kantere ◽  
V. A. Gurkin
Keyword(s):  
Environmental Factors ◽  
Kinetics Of

Elucidating the Kinetics of β-Amyloid Fibril Formation

2005 ◽  
pp. 106-118 ◽  
Author(s):  
Nadia J. Edwin ◽  
Grigor B. Bantchev ◽  
Paul S. Russo ◽  
Robert P. Hammer ◽  
Robin L. McCarley
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Kinetics Of

scholarly journals Inhibition of Protein Aggregation by Several Antioxidants

2018 ◽  
Vol 2018 ◽  
pp. 1-12 ◽  
Author(s):  
Samra Hasanbašić ◽  
Alma Jahić ◽  
Selma Berbić ◽  
Magda Tušek Žnidarič ◽  
Eva Žerovnik
Keyword(s):  
Vitamin C ◽  
Protein Aggregation ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Transmission Electron ◽  
Tht Fluorescence ◽  
Shared Property ◽  
High Concentrations ◽  
Kinetics Of

Amyloid fibril formation is a shared property of all proteins; therefore, model proteins can be used to study this process. We measured protein aggregation of the model amyloid-forming protein stefin B in the presence and absence of several antioxidants. Amyloid fibril formation by stefin B was routinely induced at pH 5 and 10% TFE, at room temperature. The effects of antioxidants NAC, vitamin C, vitamin E, and the three polyphenols resveratrol, quercetin, and curcumin on the kinetics of fibril formation were followed using ThT fluorescence. Concomitantly, the morphology and amount of the aggregates and fibrils were checked by transmission electron microscopy (TEM). The concentration of the antioxidants was varied, and it was observed that different modes of action apply at low or high concentrations relative to the binding constant. In order to obtain more insight into the possible mode of binding, docking of NAC, vitamin C, and all three polyphenols was done to the monomeric form of stefin B.

DISPROPORTIONATION AND RECOMBINATION OF CYANISOPROPYL RADICALS: REARRANGEMENT OF DIMETHYLKETENECYANISOPROPYLIMINE TO TETRAMETHYLSUCCINODINITRILE

1959 ◽  
Vol 37 (7) ◽  
pp. 1165-1169 ◽  
Author(s):  
M. Talât-Erben ◽  
A. N. Isfendiyaroğlu
Keyword(s):  
Experimental Data ◽  
Thermal Decomposition ◽  
Free Radicals ◽  
Molecular Mechanism ◽  
Reaction Scheme ◽  
Side Reactions ◽  
Minor Importance ◽  
Azo Compound ◽  
Kinetics Of ◽  
Good Agreement

Evidence is presented that the ketenimine intermediate formed in the thermal decomposition of azo-bis-isobutyronitrile (AIBN) rearranges quantitatively to tetramethylsuccinodinitrile (TMSDN), mainly by a molecular mechanism. Interpretation of experimental data on the basis of a reaction scheme consistent with the nature of the main products and the features of the kinetics of the decomposition permits estimation, by means of a simple diagram, of the extent of disproportionation, as well as that of the normal and abnormal recombination of cyanisopropyl radicals. The result obtained for the latter is in good agreement with that determined previously by an alternative method. The analysis does not exclude absolutely the possibility of side reactions in which the azo-compound partly decomposes by a molecular process, and the intermediate decomposes into free radicals. However, it is concluded that these side reactions, if any, must be of minor importance.

Kinetics of protein fibril formation: Methods and mechanisms

2017 ◽  
Vol 100 ◽  
pp. 3-10 ◽  
Author(s):  
E. Kiran Kumar ◽  
Neshatul Haque ◽  
N. Prakash Prabhu
Keyword(s):  
Fibril Formation ◽  
Protein Fibril ◽  
Kinetics Of
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