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230515 ||| eng |
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|a 9783036567808
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|a 9783036567815
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|a books978-3-0365-6780-8
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| 100 |
1 |
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|a Simon, Istvan
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| 245 |
0 |
0 |
|a Frontiers in Protein Structure Research
|h Elektronische Ressource
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| 260 |
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|a Basel
|b MDPI - Multidisciplinary Digital Publishing Institute
|c 2023
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| 300 |
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|a 1 electronic resource (352 p.)
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| 653 |
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|a α-helical bundle
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|a deep sequencing
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|a UFC1
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|a NMR
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|a quantitative prediction model
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|a protein
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|a alphafold
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|a molecular chaperones
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|a GlcNAc
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|a deep learning
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|a photosynthesis
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|a galactose
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|a multiscale modeling
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|a glucose
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|a transient complex
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|a site-directed mutagenesis
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| 653 |
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|a inter-subunit interaction
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| 653 |
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|a solvent-accessible surface area
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| 653 |
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|a xylose
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| 653 |
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|a free energy
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| 653 |
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|a FKBP12
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| 653 |
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|a retardants
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| 653 |
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|a E484Q
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| 653 |
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|a GalNAc
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| 653 |
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|a electrospray ionization mass spectrometry
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| 653 |
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|a B.1.1.7
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| 653 |
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|a circular dichroism
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| 653 |
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|a germline TP53 missense variants
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| 653 |
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|a genetic variation
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|a intrinsically disordered
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| 653 |
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|a high hydrostatic pressure
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| 653 |
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|a spike protein
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| 653 |
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|a protein-protein complex
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| 653 |
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|a iduronate
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| 653 |
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|a Research & information: general / bicssc
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| 653 |
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|a residue packing
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| 653 |
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|a Biology, life sciences / bicssc
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| 653 |
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|a prediction
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| 653 |
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|a bifidobacteria
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| 653 |
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|a configurational entropy
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| 653 |
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|a fucose
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| 653 |
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|a analytical ultracentrifugation
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| 653 |
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|a metalloprotein
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| 653 |
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|a hydrogen/deuterium exchange
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| 653 |
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|a UBA5
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| 653 |
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|a complex structure
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| 653 |
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|a Li-Fraumeni syndrome
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| 653 |
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|a protein conformation
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| 653 |
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|a ProSPr
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| 653 |
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|a mannose
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| 653 |
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|a manganese
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| 653 |
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|a protein dynamics
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| 653 |
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|a intrinsically disordered proteins
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| 653 |
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|a transmembrane proteins
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|a retrainable
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| 653 |
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|a distance
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| 653 |
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|a Shannon information entropy
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| 653 |
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|a contact
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| 653 |
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|a nitrosylation
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| 653 |
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|a saturation mutagenesis
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| 653 |
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|a oxidative folding
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| 653 |
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|a FKBP51
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| 653 |
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|a C1q
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| 653 |
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|a UFM1
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| 653 |
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|a cysteine reactivity
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| 653 |
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|a homotetramer
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| 653 |
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|a OTOL1
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| 653 |
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|a Keap1
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| 653 |
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|a T478K and L452R mutation
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| 653 |
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|a ribosomal exit tunnel
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| 653 |
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|a energy-dependent protein folding
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| 653 |
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|a mutual synergetic folding
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| 653 |
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|a thermal shift assay
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| 653 |
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|a n/a
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| 653 |
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|a CO2 concentrating mechanism
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| 653 |
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|a phosphorylation
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| 653 |
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|a small-angle X-ray scattering
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| 653 |
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|a bidirectional long-short term memory
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| 653 |
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|a protein-protein interactions
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| 653 |
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|a protein folding
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| 653 |
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|a calcium binding proteins
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| 653 |
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|a tetrabromobisphenol S
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| 653 |
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|a glutathione
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| 653 |
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|a solvent accessibility of peptide bonds
|
| 653 |
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|a nuclear magnetic resonance spectroscopy
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| 653 |
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|a mass spectrometry
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| 653 |
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|a human milk
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| 653 |
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|a Nrf2
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| 653 |
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|a FK506-binding protein
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| 653 |
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|a physical model of protein folding
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| 653 |
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|a free energy landscape
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| 653 |
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|a protein-protein binding
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| 653 |
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|a conserved domains
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| 653 |
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|a force fields
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| 653 |
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|a COVID-19
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| 653 |
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|a tetrabromobisphenol A
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| 653 |
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|a coarse-grained modeling
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| 653 |
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|a diffusion-ordered NMR spectroscopy
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| 653 |
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|a otolin-1
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| 653 |
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|a hereditary breast cancer
|
| 653 |
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|a otoconia
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| 653 |
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|a fucosidases
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| 653 |
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|a dataset
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| 653 |
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|a protein-ligand interactions
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| 653 |
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|a B.1.617.2
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| 653 |
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|a thermodynamic stability
|
| 653 |
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|a N501Y mutation
|
| 653 |
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|a Neu5Ac
|
| 653 |
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|a CASP
|
| 653 |
|
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|a entropy
|
| 653 |
|
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|a glycosyl hydrolases
|
| 653 |
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|a oxidative stress
|
| 653 |
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|a glucuronate
|
| 653 |
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|a amino acid composition
|
| 653 |
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|a convolutional neural network
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| 653 |
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|a erythrocytes
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| 653 |
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|a erythrocyte membrane
|
| 653 |
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|a glutathionylation
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| 653 |
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|a tetrahydropyran
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| 653 |
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|a co-translational protein folding
|
| 700 |
1 |
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|a Magyar, Csaba
|
| 700 |
1 |
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|a Simon, Istvan
|
| 700 |
1 |
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|a Magyar, Csaba
|
| 041 |
0 |
7 |
|a eng
|2 ISO 639-2
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| 989 |
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|b DOAB
|a Directory of Open Access Books
|
| 500 |
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|a Creative Commons (cc), https://creativecommons.org/licenses/by/4.0/
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| 028 |
5 |
0 |
|a 10.3390/books978-3-0365-6780-8
|
| 856 |
4 |
2 |
|u https://directory.doabooks.org/handle/20.500.12854/98814
|z DOAB: description of the publication
|
| 856 |
4 |
0 |
|u https://www.mdpi.com/books/pdfview/book/6860
|7 0
|x Verlag
|3 Volltext
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|a 000
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|a 333
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|a 140
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|a 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.
|