Focal contributions to molecular biophysics and structural biology: a personal view. Part II

Eisenberg, Henryk

doi:10.1016/s0301-4622(02)00164-3

Cited by 4 publications

(2 citation statements)

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“…Since the 1950s, following the discovery of the DNA double helix, applying the principle of equilibrium statistical thermodynamics to biological systems has been the central theme of biophysical chemistry, − which has led to the ultimate genomic revolution. The simple examples in this section suggest that statistical thermodynamics also has a role in studying more complex living biological systems and processes.…”

Section: Three Examplesmentioning

confidence: 99%

Open-System Nonequilibrium Steady State: Statistical Thermodynamics, Fluctuations, and Chemical Oscillations

2006

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Gibbsian equilibrium statistical thermodynamics is the theoretical foundation for isothermal, closed chemical, and biochemical reaction systems. This theory, however, is not applicable to most biochemical reactions in living cells, which exhibit a range of interesting phenomena such as free energy transduction, temporal and spatial complexity, and kinetic proofreading. In this article, a nonequilibrium statistical thermodynamic theory based on stochastic kinetics is introduced, mainly through a series of examples: single-molecule enzyme kinetics, nonlinear chemical oscillation, molecular motor, biochemical switch, and specificity amplification. The case studies illustrate an emerging theory for the isothermal nonequilibrium steady state of open systems.

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Section: Three Examplesmentioning

confidence: 99%

Open-System Nonequilibrium Steady State: Statistical Thermodynamics, Fluctuations, and Chemical Oscillations

2006

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“…Reading scientific memoires12–14 of Heini, I discover with surprise and satisfaction, how much our interest and activities run parallel, and how many of his friends and coworkers did I encounter later, when the iron curtain became easier to penetrate—just to mention Emil Reisler, Allen Minton, Bill Eaton, Paul Flory, and Rainer Jaenicke. The conclusion is that the main stream of biophysical chemistry was somehow in the air in the West and East, and similar concepts and techniques were developed parallel in both isolated realms.…”

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confidence: 99%

Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view

Závodszky

Hajdú

2013

Biopolymers

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To most physicists, it was always evident that conformational fluctuation is an inherent property of all molecules. Its existence in proteins was mentioned first by Linderström-Lang and Schellman in 1959 based on their hydrogen-deuterium exchange experiments. The "induced fit" mechanism to explain ligand-induced conformational changes was suggested by Koshland in 1958. Straub combined these two concepts in his "fluctuation fit" theory in 1964. The era of protein X-ray crystallography imposed a static view of protein structures. With proteins becoming accessible to NMR analysis, conformational dynamics could be mapped, and a new wave of dynamic interpretation of enzymatic catalysis and molecular recognition appeared. Energy landscapes, energy funnels, conformational selection, conformational distribution shifts are now frequent terms in interpreting biomolecular recognition and enzymatic catalysis. All these interpretations are based on the concept that evolution uses the conformational fluctuations of enzymes to develop efficient and dynamic catalytic machines. In a resurrection of the original "fluctuation fit" concept, it is generally recognized now that spatial and temporal events of catalysis are equally important to describe its mechanism. This special issue, dedicated to the memory of Henryk Eisenberg, prompted us to look back at the last 50 years of development of a concept that-like other important concepts-appeared, evolved and became accepted during the period covered by the scientific lifespan of Henryk.

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