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dc.contributor.editorSimon, Istvan
dc.contributor.editorMagyar, Csaba
dc.date.accessioned2023-03-07T16:33:45Z
dc.date.available2023-03-07T16:33:45Z
dc.date.issued2023
dc.identifierONIX_20230307_9783036567815_104
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/98094
dc.description.abstractIn 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.languageEnglish
dc.subject.classificationthema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TB Technology: general issuesen_US
dc.subject.classificationthema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TC Biochemical engineering::TCB Biotechnologyen_US
dc.subject.otherconfigurational entropy
dc.subject.otherforce fields
dc.subject.otherintrinsically disordered proteins
dc.subject.otherprotein folding
dc.subject.otherNMR
dc.subject.otherhigh hydrostatic pressure
dc.subject.otherthermodynamic stability
dc.subject.otherα-helical bundle
dc.subject.otherLi-Fraumeni syndrome
dc.subject.otherhereditary breast cancer
dc.subject.othergermline TP53 missense variants
dc.subject.otherquantitative prediction model
dc.subject.otherprotein conformation
dc.subject.otherprotein–protein interactions
dc.subject.otherprotein–protein binding
dc.subject.otherprotein–protein complex
dc.subject.othercoarse-grained modeling
dc.subject.othermultiscale modeling
dc.subject.otherUFM1
dc.subject.otherUBA5
dc.subject.otherUFC1
dc.subject.otherprotein-protein interactions
dc.subject.othercomplex structure
dc.subject.otheroxidative stress
dc.subject.otherNrf2
dc.subject.otherKeap1
dc.subject.othernuclear magnetic resonance spectroscopy
dc.subject.otherhydrogen/deuterium exchange
dc.subject.othermass spectrometry
dc.subject.othercircular dichroism
dc.subject.otherintrinsically disordered
dc.subject.otherbifidobacteria
dc.subject.otherfucosidases
dc.subject.otherglycosyl hydrolases
dc.subject.otherconserved domains
dc.subject.otherhuman milk
dc.subject.otheranalytical ultracentrifugation
dc.subject.otherCO2 concentrating mechanism
dc.subject.otherdiffusion-ordered NMR spectroscopy
dc.subject.otherelectrospray ionization mass spectrometry
dc.subject.otherhomotetramer
dc.subject.othermanganese
dc.subject.othermetalloprotein
dc.subject.otherphotosynthesis
dc.subject.othersmall-angle X-ray scattering
dc.subject.otherC1q
dc.subject.othercalcium binding proteins
dc.subject.othergenetic variation
dc.subject.otherotoconia
dc.subject.otherotolin-1
dc.subject.otherOTOL1
dc.subject.othersite-directed mutagenesis
dc.subject.otherthermal shift assay
dc.subject.otherB.1.1.7
dc.subject.otherB.1.617.2
dc.subject.otherCOVID-19
dc.subject.otherE484Q
dc.subject.otherT478K and L452R mutation
dc.subject.otherN501Y mutation
dc.subject.otherspike protein
dc.subject.othertetrabromobisphenol A
dc.subject.othertetrabromobisphenol S
dc.subject.othererythrocyte membrane
dc.subject.otherretardants
dc.subject.othererythrocytes
dc.subject.otherprotein–ligand interactions
dc.subject.otherprotein dynamics
dc.subject.otherFK506-binding protein
dc.subject.otherFKBP12
dc.subject.otherFKBP51
dc.subject.otheroxidative folding
dc.subject.otherglutathionylation
dc.subject.othernitrosylation
dc.subject.othercysteine reactivity
dc.subject.otherribosomal exit tunnel
dc.subject.othertransient complex
dc.subject.otherglutathione
dc.subject.otherphosphorylation
dc.subject.othertransmembrane proteins
dc.subject.othersaturation mutagenesis
dc.subject.otherdeep sequencing
dc.subject.otherresidue packing
dc.subject.otherdeep learning
dc.subject.otherconvolutional neural network
dc.subject.otherbidirectional long-short term memory
dc.subject.otherprotein
dc.subject.otherprediction
dc.subject.othercontact
dc.subject.otherdistance
dc.subject.otheralphafold
dc.subject.otherProSPr
dc.subject.otherCASP
dc.subject.otherdataset
dc.subject.otherretrainable
dc.subject.othermutual synergetic folding
dc.subject.othersolvent accessibility of peptide bonds
dc.subject.otherinter-subunit interaction
dc.subject.othersolvent-accessible surface area
dc.subject.otherShannon information entropy
dc.subject.otheramino acid composition
dc.subject.otherglucose
dc.subject.otherGlcNAc
dc.subject.othergalactose
dc.subject.otherGalNAc
dc.subject.othermannose
dc.subject.otherxylose
dc.subject.otherfucose
dc.subject.otherNeu5Ac
dc.subject.otherglucuronate
dc.subject.otheriduronate
dc.subject.othertetrahydropyran
dc.subject.otherentropy
dc.subject.otherfree energy
dc.subject.otherfree energy landscape
dc.subject.otherenergy-dependent protein folding
dc.subject.otherco-translational protein folding
dc.subject.othermolecular chaperones
dc.subject.otherphysical model of protein folding
dc.subject.othern/a
dc.titleFrontiers in Protein Structure Research
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-6780-8
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036567815
oapen.relation.isbn9783036567808
oapen.pages352
oapen.place.publicationBasel


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