Frontiers in Protein Structure Research

doi:10.3390/books978-3-0365-6780-8

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https://mdpi.com/books/pdfview/book/6860

Contributor(s)

Simon, Istvan (editor)

Magyar, Csaba (editor)

Language

English

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Abstract

In this Special Issue, we aim to represent the vibrant state of protein structure studies at the end of 2021. Recent decades have brought significant changes to the protein structure research field. Thanks to the genome projects and advances in structure determination methods, the number of solved protein structures has increased significantly. Protein structure research is experiencing a new renaissance, and in 2020 the number of deposited structures in the PDB database reached a new record. An assortment of many new frontiers are presented in this collection. A single Special Issue cannot give a comprehensive overview of a large field such as proteins science, but we aim to give a broad overview of current research.

URI

https://directory.doabooks.org/handle/20.500.12854/98814

Keywords

configurational entropy; force fields; intrinsically disordered proteins; protein folding; NMR; high hydrostatic pressure; thermodynamic stability; α-helical bundle; Li-Fraumeni syndrome; hereditary breast cancer; germline TP53 missense variants; quantitative prediction model; protein conformation; protein–protein interactions; protein–protein binding; protein–protein complex; coarse-grained modeling; multiscale modeling; UFM1; UBA5; UFC1; protein-protein interactions; complex structure; oxidative stress; Nrf2; Keap1; nuclear magnetic resonance spectroscopy; hydrogen/deuterium exchange; mass spectrometry; circular dichroism; intrinsically disordered; bifidobacteria; fucosidases; glycosyl hydrolases; conserved domains; human milk; analytical ultracentrifugation; CO2 concentrating mechanism; diffusion-ordered NMR spectroscopy; electrospray ionization mass spectrometry; homotetramer; manganese; metalloprotein; photosynthesis; small-angle X-ray scattering; C1q; calcium binding proteins; genetic variation; otoconia; otolin-1; OTOL1; site-directed mutagenesis; thermal shift assay; B.1.1.7; B.1.617.2; COVID-19; E484Q; T478K and L452R mutation; N501Y mutation; spike protein; tetrabromobisphenol A; tetrabromobisphenol S; erythrocyte membrane; retardants; erythrocytes; protein–ligand interactions; protein dynamics; FK506-binding protein; FKBP12; FKBP51; oxidative folding; glutathionylation; nitrosylation; cysteine reactivity; ribosomal exit tunnel; transient complex; glutathione; phosphorylation; transmembrane proteins; saturation mutagenesis; deep sequencing; residue packing; deep learning; convolutional neural network; bidirectional long-short term memory; protein; prediction; contact; distance; alphafold; ProSPr; CASP; dataset; retrainable; mutual synergetic folding; solvent accessibility of peptide bonds; inter-subunit interaction; solvent-accessible surface area; Shannon information entropy; amino acid composition; glucose; GlcNAc; galactose; GalNAc; mannose; xylose; fucose; Neu5Ac; glucuronate; iduronate; tetrahydropyran; entropy; free energy; free energy landscape; energy-dependent protein folding; co-translational protein folding; molecular chaperones; physical model of protein folding; n/a