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The mobility of calcium-trigger proteins and its function.

B A Levine, D C Dalgarno, M P Esnouf

Ciba Foundation Symposium

|January 1, 1983

Summary

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Cellular signals trigger rapid responses through mobile polymers. Calcium binding to EF-hand proteins initiates these fast cellular actions, involving protein reorganization and energy transfer.

Area of Science:

Biochemistry
Molecular Biology
Cellular Signaling

Background:

Cellular processes rely on rapid signal transduction and energy amplification.
Mobile polymers are crucial for fast cellular responses like calcium concentration changes and protein reorganization.

Purpose of the Study:

To explore the mechanisms of trigger activity and signal energy transfer in cellular responses.
To investigate the role of calcium binding to EF-hand proteins in initiating cellular actions.

Main Methods:

Nuclear magnetic resonance (NMR) spectroscopy was used to study protein structure and internal mobility.
Temperature dependence of NMR shifts was analyzed to understand protein dynamics.

Main Results:

Related Experiment Videos

Calcium binding to EF-hand motifs (loops between helices) initiates cellular signals.

Proteins composed of interacting helices exhibit greater internal main chain mobility compared to beta-sheet proteins.

Highly charged, loosely structured sequences are associated with signal transfer.

Conclusions:

EF-hand proteins act as key receptors for calcium binding, initiating rapid cellular responses.
Protein structure, particularly helix-loop arrangements, dictates internal mobility and signal propagation.
Mobile sequences in proteins like troponin I, T, and tropomyosin facilitate the transfer of trigger messages.