Characterization of Grp78/BiP Protein Complexes in Skeletal Muscle Using Affinity Mass Spectrometry

2017 ◽  
Vol 2 (4) ◽  
Author(s):  
Dapeng Chen ◽  
◽  
Eva R. Chin ◽  
Keyword(s):  
Mass Spectrometry ◽  
Skeletal Muscle ◽  
Protein Complexes

Characterization of In Vivo Protein Complexes via Chemical Cross-Linking and Mass Spectrometry

2021 ◽  
Author(s):  
Yuefan Wang ◽  
Yingwei Hu ◽  
Naseruddin Höti ◽  
Lan Huang ◽  
Hui Zhang
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Cross Linking ◽  
Chemical Cross Linking

Combining Electron Microscopy (EM) and Cross-Linking Mass Spectrometry (XL-MS) for Structural Characterization of Protein Complexes

2021 ◽  
pp. 217-232
Author(s):  
Lucía Quintana-Gallardo ◽  
Moisés Maestro-López ◽  
Jaime Martín-Benito ◽  
Miguel Marcilla ◽  
Daniel Rutz ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Mass Spectrometry ◽  
Structural Characterization ◽  
Protein Complexes ◽  
Cross Linking

Mass spectrometric characterization of protein structures and protein complexes in condensed and gas phase

2017 ◽  
Vol 23 (6) ◽  
pp. 445-459 ◽  
Author(s):  
Yelena Yefremova ◽  
Bright D Danquah ◽  
Kwabena FM Opuni ◽  
Reham El-Kased ◽  
Cornelia Koy ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Electrospray Mass Spectrometry ◽  
Protein Complexes ◽  
Protein Structures ◽  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Direct Access ◽  
Intact Protein

Proteins are essential for almost all physiological processes of life. They serve a myriad of functions which are as varied as their unique amino acid sequences and their corresponding three-dimensional structures. To fulfill their tasks, most proteins depend on stable physical associations, in the form of protein complexes that evolved between themselves and other proteins. In solution (condensed phase), proteins and/or protein complexes are in constant energy exchange with the surrounding solvent. Albeit methods to describe in-solution thermodynamic properties of proteins and of protein complexes are well established and broadly applied, they do not provide a broad enough access to life-science experimentalists to study all their proteins' properties at leisure. This leaves great desire to add novel methods to the analytical biochemist's toolbox. The development of electrospray ionization created the opportunity to characterize protein higher order structures and protein complexes rather elegantly by simultaneously lessening the need of sophisticated sample preparation steps. Electrospray mass spectrometry enabled us to translate proteins and protein complexes very efficiently into the gas phase under mild conditions, retaining both, intact protein complexes, and gross protein structures upon phase transition. Moreover, in the environment of the mass spectrometer (gas phase, in vacuo), analyte molecules are free of interactions with surrounding solvent molecules and, therefore, the energy of inter- and intramolecular forces can be studied independently from interference of the solvating environment. Provided that gas phase methods can give information which is relevant for understanding in-solution processes, gas phase protein structure studies and/or investigations on the characterization of protein complexes has rapidly gained more and more attention from the bioanalytical scientific community. Recent reports have shown that electrospray mass spectrometry provides direct access to six prime protein complex properties: stabilities, compositions, binding surfaces (epitopes), disassembly processes, stoichiometries, and thermodynamic parameters.

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