Frontiers in Protein Structure Research

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

dc.contributor.editor	Simon, Istvan
dc.contributor.editor	Magyar, Csaba
dc.date.accessioned	2023-04-05T12:52:27Z
dc.date.available	2023-04-05T12:52:27Z
dc.date.issued	2023
dc.identifier	ONIX_20230405_9783036567815_93
dc.identifier.uri	https://directory.doabooks.org/handle/20.500.12854/98814
dc.description.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.
dc.language	English
dc.subject.classification	bic Book Industry Communication::G Reference, information & interdisciplinary subjects::GP Research & information: general
dc.subject.classification	bic Book Industry Communication::P Mathematics & science::PS Biology, life sciences
dc.subject.other	configurational entropy
dc.subject.other	force fields
dc.subject.other	intrinsically disordered proteins
dc.subject.other	protein folding
dc.subject.other	NMR
dc.subject.other	high hydrostatic pressure
dc.subject.other	thermodynamic stability
dc.subject.other	α-helical bundle
dc.subject.other	Li-Fraumeni syndrome
dc.subject.other	hereditary breast cancer
dc.subject.other	germline TP53 missense variants
dc.subject.other	quantitative prediction model
dc.subject.other	protein conformation
dc.subject.other	protein–protein interactions
dc.subject.other	protein–protein binding
dc.subject.other	protein–protein complex
dc.subject.other	coarse-grained modeling
dc.subject.other	multiscale modeling
dc.subject.other	UFM1
dc.subject.other	UBA5
dc.subject.other	UFC1
dc.subject.other	protein-protein interactions
dc.subject.other	complex structure
dc.subject.other	oxidative stress
dc.subject.other	Nrf2
dc.subject.other	Keap1
dc.subject.other	nuclear magnetic resonance spectroscopy
dc.subject.other	hydrogen/deuterium exchange
dc.subject.other	mass spectrometry
dc.subject.other	circular dichroism
dc.subject.other	intrinsically disordered
dc.subject.other	bifidobacteria
dc.subject.other	fucosidases
dc.subject.other	glycosyl hydrolases
dc.subject.other	conserved domains
dc.subject.other	human milk
dc.subject.other	analytical ultracentrifugation
dc.subject.other	CO2 concentrating mechanism
dc.subject.other	diffusion-ordered NMR spectroscopy
dc.subject.other	electrospray ionization mass spectrometry
dc.subject.other	homotetramer
dc.subject.other	manganese
dc.subject.other	metalloprotein
dc.subject.other	photosynthesis
dc.subject.other	small-angle X-ray scattering
dc.subject.other	C1q
dc.subject.other	calcium binding proteins
dc.subject.other	genetic variation
dc.subject.other	otoconia
dc.subject.other	otolin-1
dc.subject.other	OTOL1
dc.subject.other	site-directed mutagenesis
dc.subject.other	thermal shift assay
dc.subject.other	B.1.1.7
dc.subject.other	B.1.617.2
dc.subject.other	COVID-19
dc.subject.other	E484Q
dc.subject.other	T478K and L452R mutation
dc.subject.other	N501Y mutation
dc.subject.other	spike protein
dc.subject.other	tetrabromobisphenol A
dc.subject.other	tetrabromobisphenol S
dc.subject.other	erythrocyte membrane
dc.subject.other	retardants
dc.subject.other	erythrocytes
dc.subject.other	protein–ligand interactions
dc.subject.other	protein dynamics
dc.subject.other	FK506-binding protein
dc.subject.other	FKBP12
dc.subject.other	FKBP51
dc.subject.other	oxidative folding
dc.subject.other	glutathionylation
dc.subject.other	nitrosylation
dc.subject.other	cysteine reactivity
dc.subject.other	ribosomal exit tunnel
dc.subject.other	transient complex
dc.subject.other	glutathione
dc.subject.other	phosphorylation
dc.subject.other	transmembrane proteins
dc.subject.other	saturation mutagenesis
dc.subject.other	deep sequencing
dc.subject.other	residue packing
dc.subject.other	deep learning
dc.subject.other	convolutional neural network
dc.subject.other	bidirectional long-short term memory
dc.subject.other	protein
dc.subject.other	prediction
dc.subject.other	contact
dc.subject.other	distance
dc.subject.other	alphafold
dc.subject.other	ProSPr
dc.subject.other	CASP
dc.subject.other	dataset
dc.subject.other	retrainable
dc.subject.other	mutual synergetic folding
dc.subject.other	solvent accessibility of peptide bonds
dc.subject.other	inter-subunit interaction
dc.subject.other	solvent-accessible surface area
dc.subject.other	Shannon information entropy
dc.subject.other	amino acid composition
dc.subject.other	glucose
dc.subject.other	GlcNAc
dc.subject.other	galactose
dc.subject.other	GalNAc
dc.subject.other	mannose
dc.subject.other	xylose
dc.subject.other	fucose
dc.subject.other	Neu5Ac
dc.subject.other	glucuronate
dc.subject.other	iduronate
dc.subject.other	tetrahydropyran
dc.subject.other	entropy
dc.subject.other	free energy
dc.subject.other	free energy landscape
dc.subject.other	energy-dependent protein folding
dc.subject.other	co-translational protein folding
dc.subject.other	molecular chaperones
dc.subject.other	physical model of protein folding
dc.subject.other	n/a
dc.title	Frontiers in Protein Structure Research
dc.type	book
oapen.identifier.doi	10.3390/books978-3-0365-6780-8
oapen.relation.isPublishedBy	46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn	9783036567815
oapen.relation.isbn	9783036567808
oapen.pages	352
oapen.place.publication	Basel

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