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- W2022790987 abstract "An equilibrium exists between two conformations of δ-chymotrypsin. This equilibrium is shifted when the N-terminal residue isoleucine 16 binds a proton. The two conformations, which have been previously shown to differ in their optical rotation and circular dichroism, also show different ultraviolet absorption and fluorescence spectra. The conformational transition exhibits the same apparent pK (9 at 15°) when monitored by the variations of either of these physical parameters. The kinetic behaviour of this transition has been investigated with a pH jump relaxation method. The data presented here support the hypothesis that the transition occurs between only two stable states E and E'. This transition can be summarized by the scheme:Download : Download full-size image in which the constants have the following values at 15°: Isomerization rate constants : k1 = 0.005 sec−1 ; k−1 = 0.23 sec−1 ; k2 = 3.3 sec−1 ; k−2 = 0.07 sec−1. Dissociation constants : K = 3.10−11 M (pK = 10.5) ; K' = 6.10−8 M (pK' = 7.2). The affinity of the N-terminal amino group of isoleucine 16 for the proton is therefore shifted 2,000 fold when the protein goes from one structural state to the other. Il existe un équilibre entre deux conformations de la δ-chymotrypsine. Cet équilibre est déplacé quand le résidu isoleucine N-terminal capte un proton. Les deux conformations, dont on a vu précédemment qu'elles différaient par leur pouvoir rotatoire et leur dichroïsme circulaire, différent également par leur spectre d'absorption dans l'ultra-violet et leur spectre de fluorescence. La transition de structure présente le même pK apparent (9 à 15°) quand elle est provoquée par une variation de l'un ou l'autre de ces paramètres physiques. On a étudié le comportement cinétique de cette transition par une méthode de saut de pH. Les travaux que nous exposons confirment l'hypothèse que cette transition ne se produit qu'entre deux états stables E et E'. Cette transition se résume dans le schéma:Download : Download full-size image où les constantes ont la valeur suivante à 15° : Constantes d'isomérisation : k1 = 0,005 sec−1 ; k−1 = 0,23 sec−1 ; k2 = 3,3 sec−1 ; k−2 = 0,07 sec−1. Constantes de dissociation : K = 3,10−11 M (pK = 10,5) ; K' = 6,10−8 M (pK' = 7,2). L'affinité du groupement aminé N-terminal de l'isoleucine 16 pour le proton varie donc 2 000 fois quand la protéine passe d'une structure à l'autre. Es besteht ein Gleichgewicht zwischen zwei Konformationen des δ-Chymotrypsins. Dieses Gleichgewicht wird verschoben, wenn der N-Endrest Isoleucin 16 ein Proton bindet. Diese beiden Konformationen, welche, wie früher gezeigt, durch die optische Rotation und den Dichroismus sich unterscheiden, weisen auch verschiedene Ultraviolett-Absorptions- und Fluoreszenz-Spektra auf. Die konformationelle Transition zeigt dasselbe Schein-pK (9 bei 15°), wenn sie durch beide physikalischen Parameter kontrolliert wird. Dies Transition wurde mit Hilfe der pH-Jump-Relaxationsmethode kinetisch untersucht. Die hier vorgeführten Angaben bekräftigen die Hypothese, dass die Transition nur zwischen zwei beständigen Zuständen E und E' stattfindet. Diese Transition kann durch folgender Schema zusammengefasst werden :Download : Download full-size image in welchem die Konstanten folgende Werte bei 15° zeigen: Isomerisationsgeschwindigkeits-Konstanten : k1 = 0,005 sec−1; k−1 = 0,23 sec−1; k2 = 3,3 sec−1 ; k−2 = 0,07 sec−1. Dissoziationskonstanten : K = 3.10−11 M (pK = 10,5) ; K' = 6.10−8 M (pK' = 7,2). Die Affinität der N-Endaminogruppe des Isoleucine 16 für das Protein wird also um einen Faktor 2000 geändert, wenn das Protein von einem Strukturzustand zum anderem übergeht." @default.
- W2022790987 created "2016-06-24" @default.
- W2022790987 creator A5055712923 @default.
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- W2022790987 date "1971-03-01" @default.
- W2022790987 modified "2023-10-11" @default.
- W2022790987 title "Rate of ligand-promoted isomerization of proteins. Relaxation study of the “alkaline-transition” of δ-chymotrypsin" @default.
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- W2022790987 doi "https://doi.org/10.1016/s0300-9084(71)80076-7" @default.
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