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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

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Structural stability of electrosprayed proteins: temperature and hydration effects.

Erik G Marklund¹, Daniel S D Larsson, David van der Spoel

¹Department of Cell and Molecular Biology, Uppsala University, Box 596, SE-75124, Uppsala, Sweden.

Physical Chemistry Chemical Physics : PCCP

|September 4, 2009

Summary

Electrospray ionization preserves protein structure in vacuum with a thin water layer. Molecular dynamics simulations show proteins remain stable up to 425 K, crucial for gas-phase structural studies.

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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Area of Science:

Biophysics
Computational Chemistry
Structural Biology

Background:

Electrospray ionization (ESI) is vital for gas-phase protein studies.
Maintaining protein structure during the transition to the gas phase is critical for experimental success.
The influence of temperature on protein structure in ESI is not fully understood.

Purpose of the Study:

To investigate the effect of temperature and hydration on protein structure during gas-phase transition.
To determine the minimum hydration level required for structural preservation.
To assess protein stability across a range of temperatures using molecular dynamics.

Main Methods:

Molecular dynamics simulations of four sparingly hydrated globular proteins (Trp-cage, Ctf, ubiquitin, lysozyme).
Simulations conducted in vacuum at temperatures from 225 K to 425 K.
Utilized OPLS-AA/L, AMBER03, and GROMOS96 53a6 force fields for cross-validation.

Main Results:

A 3 Å water layer effectively preserves protein structure in vacuum up to 425 K for most proteins studied.
Ctf exhibited minor secondary structure changes at lower temperatures.
Water molecules formed clusters and patterns on protein surfaces, maintaining hydrogen bond networks.

Conclusions:

Limited hydration and specific temperature ranges are key to preserving protein structure for gas-phase analysis.
Findings support the feasibility of single-particle imaging experiments.
The choice of force field had minimal impact on the observed structural stability.