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Protein Dynamics in Living Cells01:19

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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Related Experiment Video

Updated: Jul 18, 2025

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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K-Pro: Kinetics Data on Proteins and Mutants.

Paola Turina1, Piero Fariselli2, Emidio Capriotti1

  • 1Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Via F. Selmi 3, 40126 Bologna, Italy.

Journal of Molecular Biology
|August 25, 2023
PubMed
Summary
This summary is machine-generated.

K-Pro is a new database that collects experimental protein folding kinetic data for monomeric proteins. This resource aids in understanding protein folding mechanisms and human diseases caused by misfolded proteins.

Keywords:
folding kineticsfolding rate constantprotein foldingprotein varianttransition state

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Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Protein folding is vital for protein function and understanding genetic links to phenotypes.
  • Misfolded proteins are implicated in various human diseases, necessitating research into folding mechanisms.
  • Experimental kinetic and thermodynamic data on protein folding are crucial for this research.

Purpose of the Study:

  • To introduce K-Pro, a novel database for collecting and storing experimental kinetic data on protein folding.
  • To provide a comprehensive resource for researchers studying protein folding kinetics and thermodynamics.
  • To facilitate the understanding of protein folding mechanisms and their relation to human disorders.

Main Methods:

  • Development of a dedicated database, K-Pro, for experimental kinetic data of monomeric proteins with a two-state folding mechanism.
  • Curating and storing 1,529 records from 62 proteins (65 structures) including folding/unfolding rates, Tanford's β, and ϕ values.
  • Integration of thermodynamic parameters where available and cross-linking to external databases (PDB, UniProt, PubMed).

Main Results:

  • K-Pro houses extensive kinetic data, including logarithmic folding/unfolding rates, Tanford's β, and ϕ values for 62 proteins.
  • The database contains 1,529 records and includes thermodynamic data when available.
  • A user-friendly interface allows easy browsing, downloading, and visualization of protein and mutant data.

Conclusions:

  • K-Pro serves as a valuable, freely accessible resource for protein folding research.
  • The database supports the study of protein folding kinetics and thermodynamics, aiding in the investigation of protein misfolding diseases.
  • K-Pro's integrated data and user-friendly interface enhance accessibility and utility for the scientific community.