Sign in to use this feature.

Years

Between: -

Subjects

remove_circle_outline
remove_circle_outline

Journals

Article Types

Countries / Regions

Search Results (2)

Search Parameters:
Keywords = KNF model

Order results
Result details
Results per page
Select all
Export citation of selected articles as:
14 pages, 2020 KB  
Review
Biological Calorimetry: Old Friend, New Insights
by Olga Abian, Sonia Vega and Adrian Velazquez-Campoy
Biophysica 2023, 3(1), 21-34; https://doi.org/10.3390/biophysica3010002 - 20 Jan 2023
Cited by 8 | Viewed by 4590
Abstract
Calorimetry is an old experimental technique (first instrument developed in S. XVIII), but it is broadly used and still provides key information for understanding biological processes at the molecular level, particularly, cooperative phenomena in protein interactions. Here, we review and highlight some key [...] Read more.
Calorimetry is an old experimental technique (first instrument developed in S. XVIII), but it is broadly used and still provides key information for understanding biological processes at the molecular level, particularly, cooperative phenomena in protein interactions. Here, we review and highlight some key aspects of biological calorimetry. Several biological systems will be described in which calorimetry was instrumental for modeling the behavior of the protein and obtaining further biological insight. Full article
(This article belongs to the Special Issue State-of-the-Art Biophysics in Spain)
Show Figures

Figure 1

22 pages, 2442 KB  
Article
Structural Basis of Sequential and Concerted Cooperativity
by Veronica Morea, Francesco Angelucci, Jeremy R. H. Tame, Enrico Di Cera and Andrea Bellelli
Biomolecules 2022, 12(11), 1651; https://doi.org/10.3390/biom12111651 - 7 Nov 2022
Cited by 6 | Viewed by 4204
Abstract
Allostery is a property of biological macromolecules featuring cooperative ligand binding and regulation of ligand affinity by effectors. The definition was introduced by Monod and Jacob in 1963, and formally developed as the “concerted model” by Monod, Wyman, and Changeux in 1965. Since [...] Read more.
Allostery is a property of biological macromolecules featuring cooperative ligand binding and regulation of ligand affinity by effectors. The definition was introduced by Monod and Jacob in 1963, and formally developed as the “concerted model” by Monod, Wyman, and Changeux in 1965. Since its inception, this model of cooperativity was seen as distinct from and not reducible to the “sequential model” originally formulated by Pauling in 1935, which was developed further by Koshland, Nemethy, and Filmer in 1966. However, it is difficult to decide which model is more appropriate from equilibrium or kinetics measurements alone. In this paper, we examine several cooperative proteins whose functional behavior, whether sequential or concerted, is established, and offer a combined approach based on functional and structural analysis. We find that isologous, mostly helical interfaces are common in cooperative proteins regardless of their mechanism. On the other hand, the relative contribution of tertiary and quaternary structural changes, as well as the asymmetry in the liganded state, may help distinguish between the two mechanisms. Full article
Show Figures

Figure 1

Back to TopTop