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Hydration of clupeine in solution.

M Ishimura¹, N Nishi, H Uedaira

¹Research Institute for Polymers and Textiles, Ibaraki, Japan.

International Journal of Peptide and Protein Research

|May 1, 1991

Summary

Spin-lattice relaxation times revealed that clupeine, a protein, exhibits a random conformation in aqueous solutions. This finding was supported by analyzing its constituent amino acids and their hydration properties.

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Area of Science:

Biophysics
Physical Chemistry
Molecular Dynamics

Background:

Understanding protein conformation in solution is crucial for various biological processes.
Spin-lattice relaxation time (T1) is a sensitive probe of molecular dynamics and hydration.

Purpose of the Study:

To investigate the solution conformation of clupeine using spin-lattice relaxation times.
To determine the dynamic hydration numbers and rotational correlation times of water molecules around clupeine and its constituent amino acids.

Main Methods:

Measurement of spin-lattice relaxation times (T1) for H2(17)O in aqueous solutions of clupeine and its amino acids (serine, threonine, proline, arginine) at 25°C.
Determination of dynamic hydration numbers (nDHN) from the concentration dependence of T1.
Estimation of coordination numbers (nh) and rotational correlation times (tau ch) of water molecules.

Main Results:

The dynamic hydration number of clupeine was consistent with the sum of its constituent amino acids' hydration numbers.
The rotational correlation time ratio (tau ch/tau co) for clupeine was 1.85, similar to arginine.
Water molecules around clupeine showed dynamics comparable to those around arginine.

Conclusions:

Clupeine adopts a random coil conformation in aqueous solution.
The hydration properties of clupeine can be predicted from its constituent amino acids.
The study provides insights into protein hydration and molecular dynamics in solution.

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