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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Other Glycolytic Pathways01:24

Other Glycolytic Pathways

The pentose phosphate pathway (PPP) operates in parallel with glycolysis, facilitating the metabolism of both pentoses and glucose. This pathway consists of two distinct phases: the oxidative and non-oxidative phases. While it does not directly generate ATP, the intermediates formed during the process can integrate into glycolysis, contributing to cellular energy metabolism when required.Oxidative Phase: NADPH ProductionThe oxidative phase of the pentose phosphate pathway is primarily...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: May 22, 2026

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

Protein flexibility and enzymatic catalysis.

M Kokkinidis1, N M Glykos, V E Fadouloglou

  • 1Department of Biology, University of Crete, Heraklion, Crete, Greece.

Advances in Protein Chemistry and Structural Biology
|May 22, 2012
PubMed
Summary
This summary is machine-generated.

Protein structural dynamics are crucial for biological function, influencing interactions and enzymatic activity. Understanding protein flexibility is key to unlocking new therapeutic and biotechnological applications.

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Last Updated: May 22, 2026

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Protein structures are inherently dynamic, exhibiting local flexibility and global plasticity.
  • This dynamic nature is fundamental to various biological processes, including protein interactions, signal transduction, and enzyme function.

Purpose of the Study:

  • To explore the critical role of protein flexibility in biological functions.
  • To highlight enzymes as model systems for studying protein dynamics and their impact on biological activity.

Main Methods:

  • The study is primarily a review and synthesis of existing knowledge on protein dynamics.
  • It analyzes the implications of protein fluctuations and conformational changes.

Main Results:

  • Protein flexibility is essential for enzyme catalysis, affecting active site dynamics, substrate binding, and product release.
  • Conformational flexibility influences reaction rates, substrate turnover, and the stabilization of reaction intermediates.

Conclusions:

  • Protein flexibility is an intrinsic property vital for enzyme function and biological processes.
  • Further research into protein dynamics can lead to advancements in enzyme engineering and drug development.