Conformation Changes of Proteins

Lumry, Rufus; Eyring, Henry

doi:10.1021/j150512a005

Cited by 832 publications

(483 citation statements)

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“…In fact, the thermally induced unfolding of many proteins has been shown to be occasionally followed by an irreversible process that induces aggregation (Sanchez-Ruiz et al 1988;Azuaga et al 2002;Rezaei et al 2002;Weijers et al 2003;Michnik et al 2005). Generally, such aggregation has been modeled as shown in Scheme 1, where N, U, and A are native, unfolded, and irreversible unfolded protein forms, respectively (Lumry and Eyring 1954;Sanchez-Ruiz et al 1988;Azuaga et al 2002;Rezaei et al 2002;Weijers et al 2003;Michnik et al 2005). The model consists of the reversible folding/unfolding transition (N ⇌ U) of the protein and the subsequent aggregation of non-native species that has been traditionally considered an essentially irreversible process.…”

Section: Thermally Induced Aggregation Of Proteinsmentioning

confidence: 99%

Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

Sasahara

Goto

2012

Biophys Rev

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The aggregation of proteins into amyloid fibrils is a topic that has attracted great interest because the process is associated with the pathology of numerous human diseases. Despite considerable progress in the elucidation of the structure of amyloid fibrils and the kinetic mechanism of their formation, knowledge on the thermodynamic aspects underlying the formation and stability of amyloid fibrils is limited. In this review, we summarize recent calorimetric studies of amyloid fibril formation, with the goal of obtaining a better understanding of the causal factors that thermally induce proteins to aggregate into amyloid fibrils. Calorimetric data show that differential scanning calorimetry is a useful technique to study the causative factors that thermally trigger the conversion to the amyloid structure and highlight the physics related to the thermal fluctuation of proteins during this conversion.

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Section: Thermally Induced Aggregation Of Proteinsmentioning

confidence: 99%

Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

Sasahara

Goto

2012

Biophys Rev

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“…The mechanism of enzyme denaturation can have different stages and complexities, the most common models, described by first order kinetics, being those developed by Arrhenius and/or Lumry & Eyring (Fogler, 1999;Lumry and Eyring, 1954). However, in some cases, an apparently simple, first-order inactivation can mask a set of complex molecular events.…”

Section: Introductionmentioning

confidence: 99%

Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Aguiar‐Oliveira

Maugeri

2011

Braz. J. Chem. Eng.

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-The thermal stability of the extracellular fructosyltransferase (FTase) from Rhodotorula sp., recovered from cultivation medium by ethanol precipitation and immobilized onto niobium ore, was studied by Arrhenius plot, half-life profile, half-inactivation temperature (T 50 ) and thermodynamic parameters. The Arrhenius plot showed two different behaviors with different deactivation energies (E ad ) only after immobilization, the transition occurring in the temperature interval between 51 and 52°C. T 50 for the free enzyme was estimated to be around 62°C and, after immobilization, 66°C. After 15 minutes at 52°C, it was also possible to observe enzymatic activation for both the free and immobilized forms, but greater activation was achieved at pH 4.5 with the immobilized enzyme. Between 47-51°C the immobilized enzyme was more stable than the free enzyme, with pH 6.0 being the more stable condition for the immobilized enzyme. However, above 52°C the free form was more stable.

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“…This model is usually known as the Lumry-Eyring mechanism (Lumry and Eyring 1954;Sanchez-Ruiz 2010). According to the relative values of the kinetic coefficients, two main scenarios can be envisaged (Sanchez-Ruiz 1992).…”

Section: Kinetic Stability: the Two-state Irreversible Modelmentioning

confidence: 99%

Kinetic stability of membrane proteins

2017

Biophys Rev

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Although membrane proteins constitute an important class of biomolecules involved in key cellular processes, study of the thermodynamic and kinetic stability of their structures is far behind that of soluble proteins. It is known that many membrane proteins become unstable when removed by detergent extraction from the lipid environment. In addition, most of them undergo irreversible denaturation, even under mild experimental conditions. This process was found to be associated with partial unfolding of the polypeptide chain exposing hydrophobic regions to water, and it was proposed that the formation of kinetically trapped conformations could be involved. In this review, we will describe some of the efforts toward understanding the irreversible inactivation of membrane proteins. Furthermore, its modulation by phospholipids, ligands, and temperature will be herein discussed.

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Conformation Changes of Proteins

Cited by 832 publications

References 6 publications

Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp

Kinetic stability of membrane proteins

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