Current methods in structural proteomics and its applications in biological sciences

Abstract

A broad working definition of structural proteomics (SP) is that it is the process of the high-throughput characterization of the three-dimensional structures of biological macromolecules. Recently, the process for protein structure determination has become highly automated and SP platforms have been established around the globe, utilizing X-ray crystallography as a tool. Although protein structures often provide clues about the biological function of a target, once the three-dimensional structures have been determined, bioinformatics and proteomics-driven strategies can be employed to derive their biological activities and physiological roles. This article reviews the current status of SP methods for the structure determination pipeline, including target selection, isolation, expression, purification, crystallization, diffraction data collection, structure solution, refinement and functional annotation.

Emerging Diagnostic and Therapeutic Potentials of Human Hair Proteomics

“…Moreover, studies have demonstrated the importance of mechanical responses, structure, and biological functions of human tissues in understanding diseases such as arthritis, atherosclerosis, and asthma . The fields of structural proteomics permits high‐throughput determination of atomic resolution of hair protein structure on a genome‐wide scale . It also permits high‐throughput automated determination of structure and annotation of individual hair protein components and the complexes they form .…”

“…It also permits high‐throughput automated determination of structure and annotation of individual hair protein components and the complexes they form . Beside MS based structural proteomics methodologies, other approaches such as NMR (for structures <25 KDa) and X‐ray crystallography can be used for high atomic resolution structure determination . An NMR‐based method known as transverse relaxation optimized spectroscopy can be used to identify structure of proteins around 50 KDa by means of pulsed sequences .…”

“…As pertains to other ‘omics field, structural proteomics is highly bioinformatics dependent. Computational biology is required to map protein sequences to structures and function to model building by homology and network based inferences . In addition, 3D protein structures as well as folding information in small subset of proteins can be determined using structural proteomics .…”

Comparison of Peptide Ion Conformers Arising from Non-Helical and Helical Peptides Using Ion Mobility Spectrometry and Gas-Phase Hydrogen/Deuterium Exchange

“…The rapid increase in the number of experimentally-determined protein structures over the last three decades [15, 16] has significantly enabled protein structure prediction capabilities. Perhaps, the simplest conception is to use sequence homology based on comparisons to known structures to infer structural elements for proteins of interest [17–19].…”

Growth of Diffraction-Quality Protein Crystals Using a Harvestable Microfluidic Device

“…1 Even once a condition for protein crystallization is identified, not all crystals will be of high quality, meaning single and well-ordered crystals that diffract to suitable resolution with low mosaicity. Common methods to crystallize proteins include vapor diffusion, batch crystallization, and seeding.…”