Average protein density is a molecular-weight-dependent function. - Wikidata - wikimedia - TriplyDB

Average protein density is a molecular-weight-dependent function.

Average protein density is a molecular-weight-dependent function.

http://www.wikidata.org/entity/Q43104992

about

LipL41, a hemin binding protein from Leptospira santarosai serovar Shermani The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9)Metabolomics and systems pharmacology: why and how to model the human metabolic network for drug discovery Protein P7 of the cystovirus φ6 is located at the three-fold axis of the unexpanded procapsid.The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex Interactions and Oligomerization of Hantavirus Glycoproteins Structure of the recombinant BPTI/Kunitz-type inhibitorrShPI-1A from the marine invertebrateStichodactyla helianthus Structural analysis of trimeric phospholipase A2 neurotoxin from the Australian taipan snake venom Quantifying the effects of elastic collisions and non-covalent binding on glutamate receptor trafficking in the post-synaptic density Intracellular water exchange for measuring the dry mass, water mass and changes in chemical composition of living cells Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugation NMR-detected brownian dynamics of αB-crystallin over a wide range of concentrations.Influence of Coulombic repulsion on the dissociation pathways and energetics of multiprotein complexes in the gas phase.Electron cryomicroscopy of membrane proteins: specimen preparation for two-dimensional crystals and single particles.Aromatic claw: A new fold with high aromatic content that evades structural prediction.Dissimilar interaction of CB1/CB2 with lipid bilayers as revealed by molecular dynamics simulation.Aging-related viscoelasticity variation of tendon stem cells (TSCs) characterized by quartz thickness shear mode (TSM) resonators Molecular modelling of the mass density of single proteins.Assembly of Weibel-Palade body-like tubules from N-terminal domains of von Willebrand factor Controlling the spatial organization of cells and extracellular matrix proteins in engineered tissues using ultrasound standing wave fields.Amelogenin nanoparticles in suspension: deviations from spherical shape and pH-dependent aggregation Internal Dynamics of a Coarse-Grained Protein Using Analytical Harmonic Representation.Ultrabroadband infrared nanospectroscopic imaging.Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin.EM∩IM: software for relating ion mobility mass spectrometry and electron microscopy data.Revisiting the interpretation of casein micelle SAXS data.Protein reactions with surface-bound molecular targets detected by oblique-incidence reflectivity difference microscopes.NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein Morphological and biochemical changes in Pseudomonas fluorescens biofilms induced by sub-inhibitory exposure to antimicrobial agents.Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy.Nuclear pore complex protein sequences determine overall copolymer brush structure and function.Label-free biomarker sensing in undiluted serum with suspended microchannel resonators Phase transitions in human IgG solutions.Three-dimensional structure of basal body triplet revealed by electron cryo-tomography.polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction Cloning, functional characterization and genomic organization of 1,8-cineole synthases from Lavandula.Thermal aggregation of recombinant protective antigen: aggregate morphology and growth rate Characterization of cement float buoyancy in the stalked barnacle Dosima fascicularis (Crustacea, Cirripedia).

P2860

Q21090667-A338A182-1E49-4D46-AB95-823B2F6ECD3E Q24312481-F87B8016-6B17-44CF-9F30-B48576C45642 Q27144251-06431B8E-2509-4B42-BFD8-ED18E907DB16 Q27313941-801FE0CC-120B-42E5-BF0E-F4CA2C319E4B Q27320362-11EE228B-53D2-46C0-83E9-D0EC10328243 Q27333529-5BCF851B-A2CC-4317-B24D-32BADC9D60C4 Q27490540-D69995F3-958C-444A-B453-F498B71B14CB Q27675071-100129A9-9C10-4911-A6F4-F486C20F5839 Q27681730-F569DC1C-AE0A-4B56-A801-05303687B7A6 Q28473916-88722F55-014D-42E4-A762-6AB5C2F8CCD8 Q28534481-2EB79BAA-897C-4538-8A66-7EE820B905D2 Q28732085-768BA5FC-90C6-4837-87E9-4C5572A84416 Q30316863-33434930-C866-46CC-882C-CEDE3A7D73DC Q30359060-107AE17A-1B36-494E-B57A-31967090F8AE Q30392211-73D916DA-51A1-4179-B14B-93C4148C2B57 Q30394199-0F69DE5C-D66C-4DD1-AC6B-B6A9A998859E Q30397741-05ADA19B-3331-423F-88F7-0E670D2B825F Q30405466-5478E990-77BC-447C-A6FA-994D3470226C Q30418179-47C76D43-5A10-4D2E-840A-A7BAD0295A4D Q30443824-8014CCBC-63B2-4A37-A2F8-9C0B375A9126 Q30473380-0A3296F1-D078-44E7-83D2-74DCB16C4D60 Q30483438-A706D486-4ED7-46D0-B97B-F3F184E31388 Q30497893-7ACB975A-6773-4F0D-9CB3-51955571EFEB Q30578882-486B6877-2F83-4FC2-AF3A-8F2E00F3DB11 Q30610715-54046674-0DB1-40A9-B9A3-71FC41C6B5C2 Q30814714-F7851D4C-0245-4D1B-948E-43AE449A1B9D Q31029161-67B5ECF4-1DAF-4061-9A77-D9B3DC2CF313 Q31119641-ED6C3C85-A3E8-43E7-ABE6-6ED26982FD16 Q33345202-B397EF4B-819B-4C02-959D-2DC1E5D8E317 Q33409233-D541F037-35FA-43A2-A197-E10180BD5AB9 Q33419303-E35B7DE9-2DDB-402E-B985-BD3CF35385BB Q33527484-F201EF48-84D3-47ED-B0B5-6C22385C5D5B Q33595850-F2132B75-DE44-4B70-898B-8B8043A1E54C Q33761414-8A5221C3-32C1-44B7-87D2-0748664FC654 Q33941043-5BD30A27-82DF-48C9-BDB3-4B77FEC131F9 Q34096396-BD93A2C3-2718-4058-8703-A9C729336516 Q34098314-0DB43F2E-AC22-4F2F-90BE-C91CA1674204 Q34271988-5AA80848-2F2E-4644-856C-C3AB8A4246B9 Q34615921-AD83BE74-9EA8-4517-A38D-1451BC4B2697 Q34768695-577A0EFB-D144-4D85-AFED-6FC3A6BE2011

P2860

Average protein density is a molecular-weight-dependent function.

http://www.wikidata.org/entity/Q43104992

description

2004 nî lūn-bûn

@nan

2004 թվականի հոկտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

name

Average protein density is a molecular-weight-dependent function.

@en

Average protein density is a molecular-weight-dependent function.

@nl

type

label

Average protein density is a molecular-weight-dependent function.

@en

Average protein density is a molecular-weight-dependent function.

@nl

prefLabel

Average protein density is a molecular-weight-dependent function.

@en

Average protein density is a molecular-weight-dependent function.

@nl

P1433

Q43104992-F0A51F45-67C8-4E5C-9382-2055309B0246

P1476

Q43104992-5738D848-0AF9-473F-A1D1-DC117AB350E7

P2093

Q43104992-A9318C5E-4F6D-4353-8B4F-C4216C32C247

P2860

Q43104992-011AF2E2-6F4B-4A15-8DEC-F611D7F05E81

Q43104992-0E9FECC5-A284-44AE-AF69-2310D57C0A90

Q43104992-46FDE257-33C0-4088-BFE9-6ACBBA202C70

Q43104992-48967FB6-688E-4777-9AB5-0F21F054BAC3

Q43104992-58537F26-8931-4387-9D7F-221AEA4C55BA

Q43104992-6F3D0A8F-7713-4244-9217-D5F6C7D07236

Q43104992-715D7614-8C02-4762-8858-6BBCC0544EF9

Q43104992-B36D729E-6A12-400C-98BC-E48DB793AEEC

Q43104992-E6812AA7-D64A-4B02-89B2-3C42E8BCEC9A

Q43104992-F6A076E0-4441-4860-9C7C-8306176A066D

P304

Q43104992-8E154A2C-7479-4C3A-B0FD-3E21F1E14846

P31

Q43104992-7D3CBE1B-B57A-4C78-BE18-F347731BF179

P356

Q43104992-A9659652-6450-4F33-AC12-5A821A1CF857

P433

Q43104992-A972344A-0E67-4E68-8118-B8F0A4A45EEA

P478

Q43104992-BD27EB02-6CA4-4F5F-814B-F71AB0948C71

P50

Q43104992-1FBE3E75-789F-49D1-8D73-796ADD4C615B

Q43104992-B4FB7231-AE78-49DC-B411-2B4AA6333000

P577

Q43104992-3717A346-8AE1-4B58-825C-49E6CB33EB2F

P5875

Q43104992-130425C1-E87F-4451-9836-A7E5C6EB500C

P698

Q43104992-1C0A526A-E3D9-4DF0-90D8-B1FC19D36D6B

P932

Q43104992-FE4C2A32-71FA-4C98-92B3-FACBF1EE9C18

P356

P1433

Protein Science

P1476

Average protein density is a molecular-weight-dependent function

@en

P2093

Hannes Fischer

http://www.w3.org/2001/XMLSchema#string

P2860

The Protein Data Bank

Modern analytical ultracentrifugation in protein science: a tutorial review

Methods used in the structure determination of bovine mitochondrial F1 ATPase

Solvent content of protein crystals

The molecular surface package

Resolution of phase ambiguity in macromolecular crystallography

The packing density in proteins: standard radii and volumes.

Are proteins well-packed?

Protein hydration in solution: experimental observation by x-ray and neutron scattering.

Accurate calculation of the density of proteins.

P304

2825-2828

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1110/PS.04688204

http://www.w3.org/2001/XMLSchema#string

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

13

http://www.w3.org/2001/XMLSchema#string

P50

Igor Polikarpov

Aldo F Craievich

P577

2004-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8326094

http://www.w3.org/2001/XMLSchema#string

P698

15388866

http://www.w3.org/2001/XMLSchema#string

P932

2286542

http://www.w3.org/2001/XMLSchema#string