Interfaces and the driving force of hydrophobic assembly. - Wikidata - wikimedia - TriplyDB

Interfaces and the driving force of hydrophobic assembly.

Interfaces and the driving force of hydrophobic assembly.

http://www.wikidata.org/entity/Q34455286

about

Potentials of mean force for protein structure prediction vindicated, formalized and generalized Water in cavity-ligand recognition.Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires Mechanisms of virus assembly Biomolecular electrostatics and solvation: a computational perspective Physicochemical characteristics of nanomaterials that affect pulmonary inflammation Thermodynamics and solvent linkage of macromolecule-ligand interactions Folding and Stabilization of Native-Sequence-Reversed Proteins.A Superamphiphobic Sponge with Mechanical Durability and a Self-Cleaning Effect.Origin of Heat Capacity Changes in a “Nonclassical” Hydrophobic Interaction Completing the family portrait of the anti-apoptotic Bcl-2 proteins: crystal structure of human Bfl-1 in complex with Bim The 1.4 Å resolution structure ofParacoccus pantotrophuspseudoazurin Protein–Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface Area Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin Protein–ligand interactions: Probing the energetics of a putative cation–π interaction Challenges and breakthroughs in recent research on self-assembly Statistical analysis of crystallization database links protein physico-chemical features with crystallization mechanisms Unusual Salt and pH Induced Changes in Polyethylenimine Solutions Matched Peptides: Tuning Matched Molecular Pair Analysis for Biopharmaceutical Applications Towards a structural biology of the hydrophobic effect in protein folding Necessity of capillary modes in a minimal model of nanoscale hydrophobic solvation Quantitative theory of hydrophobic effect as a driving force of protein structure Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes.Implicit modeling of nonpolar solvation for simulating protein folding and conformational transitions.Hydrophobe-water interactions: methane as a model Probabilistic models and machine learning in structural bioinformatics.Changes in hydration structure are necessary for collective motions of a multi-domain protein.Probing hydrophilic interface of solid/liquid-water by nanoultrasonics Emerging technologies for assembly of microscale hydrogels.Carbon Nanotubes in Biology and Medicine: In vitro and in vivo Detection, Imaging and Drug Delivery.Water-membrane partition thermodynamics of an amphiphilic lipopeptide: an enthalpy-driven hydrophobic effect.Determination of the transition-state entropy for aggregation suggests how the growth of sickle cell hemoglobin polymers can be slowed.Systematic determination of order parameters for chain dynamics using diffusion maps.Hydration dynamics at fluorinated protein surfaces Active microrheology and simultaneous visualization of sheared phospholipid monolayers Solvent fluctuations in hydrophobic cavity-ligand binding kinetics.Caffeine and sugars interact in aqueous solutions: a simulation and NMR study.Collagen unfolding accelerates water influx, determining hydration in the interstitial matrix.Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment.

P2860

Q21562146-C91CAE5E-335B-4838-AA08-1AE5A98EA81F Q24618521-FE400967-C72A-4B69-8FA9-4CFC08B6E633 Q24628864-6A8D487F-B6A1-4E3B-9C94-DF310C235EDD Q26852826-C1A8B52B-9DC7-42FF-9C5D-D09D8EB43276 Q26853115-F9CF8340-EAAC-4D49-A780-6A955D2BA8DF Q26859438-7FA1767F-2BE1-4AFE-B0EE-AC5C80F46CAA Q27024230-7CBAF1F7-E6D9-4D5D-B647-DC21B354312F Q27318306-342E5837-8E95-4DCC-83E2-B3AF38BA1C4D Q27324754-47D27AA7-51D9-4A09-B702-06658CF02FEE Q27646631-41FBB059-0570-4FB6-9F2F-CD3F66CEBD05 Q27652276-6485A93E-7042-412B-94D4-41E2A2BCEBA9 Q27662082-2E55A69E-F3D7-465B-B47C-79FED2401B0F Q27675114-9EB09AD7-319E-4A28-978C-059045351F85 Q27675123-0D86824E-A0D6-49F6-B5B3-534F5DA5D259 Q27683691-31B64595-01E3-479C-A7D9-7E1545A2ED01 Q27683926-DD1C876A-45E5-4052-87AD-DA5EEBD72BA8 Q28279677-AA18174E-54FE-450F-8ADF-73CF0445DD15 Q28540267-59C0F593-4CAB-4952-8478-3F4A270268CE Q28554398-D105C487-32CF-495A-B039-7F79A1CEDEDA Q28607086-648CF042-9D80-4F77-B938-0B8FF35D9DFF Q28828746-3EFE5AE6-DAFB-4E97-81E8-D825A66CE78D Q28834342-1BF2E972-80EA-4DAB-BA33-DD22CCCFF956 Q30357723-3971ADE3-1722-4207-94D8-68B7CBFC12D1 Q30362502-F8684B10-09F3-4842-B442-C2885750B9F3 Q30367039-1C24401F-FBFE-4660-BCEF-59E4802B4007 Q30371163-07D35320-D920-4368-8897-BD133CFB7AB4 Q30374428-3A46418A-11D8-41F1-A182-F2CBD0F1F76B Q30388209-089F2C7E-2B20-4B9E-ACD0-B88F333C3C35 Q30431650-B5A0BF69-A98E-4664-91FB-88506BC9D96D Q30449264-53AA0E84-F946-4D90-A9FD-EED30DEF6774 Q30483216-6E67E9FE-B03E-49E4-B3BF-D93C4EBD903F Q30483693-3CF43E07-9494-43A2-AB5F-769C6ED19307 Q30490510-69C28615-EA8D-4797-BD3D-0C9D664C5D6D Q30496093-09416C3D-652D-478B-A791-390BF5CFCB79 Q30496888-76696C33-F6A8-4707-9A70-121C7F9FF3CB Q30501032-C46206DE-70FC-4C83-8E3B-7B638F520CC6 Q30533272-C97AAC4D-9AF8-433B-B921-0422B6D34F4F Q30557836-09FBC17D-86E4-4C33-8D70-6CD9AED8602F Q30579475-909E924D-E392-4840-9EA1-7DA91222594B Q30583940-D9A17572-4C25-4F83-BB7B-E5C716CB12BD

P2860

Interfaces and the driving force of hydrophobic assembly.

http://www.wikidata.org/entity/Q34455286

description

2005 nî lūn-bûn

@nan

2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Interfaces and the driving force of hydrophobic assembly.

@ast

Interfaces and the driving force of hydrophobic assembly.

@en

Interfaces and the driving force of hydrophobic assembly.

@nl

type

label

Interfaces and the driving force of hydrophobic assembly.

@ast

Interfaces and the driving force of hydrophobic assembly.

@en

Interfaces and the driving force of hydrophobic assembly.

@nl

prefLabel

Interfaces and the driving force of hydrophobic assembly.

@ast

Interfaces and the driving force of hydrophobic assembly.

@en

Interfaces and the driving force of hydrophobic assembly.

@nl

P1433

Q34455286-54CE619D-7686-444E-810C-03BD3DDF1FEC

P1476

Q34455286-A82FB4FA-7F60-4CC5-AD4E-9CD4C533A69B

P2093

Q34455286-3281E4BC-18A2-4C00-805D-3AB5AAF6F178

P2860

Q34455286-1BEEC848-13D8-4FA4-96AE-52F30DCB03FC

Q34455286-21EA244C-7CBD-494D-87F7-FF1FA76638B2

Q34455286-2A9B8326-22E1-4C18-AA9C-2BEF39125AF6

Q34455286-2C061478-A98F-4352-A64E-09A5126A46E7

Q34455286-35CB666E-906A-4448-BBAE-AAC4BE25794F

Q34455286-6F75FD1B-719B-4875-A9D1-DF5B75DCF0F5

Q34455286-830E1DA9-4E9F-4D7F-8FB4-99692872CAC4

Q34455286-8870922B-DCAF-4203-A815-4D9E1A35A5A5

Q34455286-8EF85463-7886-401F-9D57-D8727FF9D372

Q34455286-91AE2A98-46D5-40FD-B0F7-763F67608DCF

P2888

Q34455286-0D0DD628-0784-4BAF-8692-6E96B46D92EC

P304

Q34455286-43058D3D-9E67-4266-9F78-A454C5E320A0

P31

Q34455286-8B88AE5A-CA5C-4A7C-AECD-1C2D81C9FBFA

P356

Q34455286-E09F1FA4-3AEF-4B32-9C6A-AC7A85D9C15A

P407

Q34455286-8020A88D-EBC8-4D0D-9F4F-31863C0CE8E2

P433

Q34455286-4EB36DEE-4907-418D-A134-BA68808ED696

P478

Q34455286-23BCB4B2-8D39-479C-BE34-E626A80A051F

P577

Q34455286-3A7E79F5-E6E4-41D7-9A9A-4461CC8D9F8D

P5875

Q34455286-ACA6EDB7-4BDA-43D4-BFF5-A1CB757FE520

P6179

Q34455286-2622B0F5-2CC8-4C79-83C1-B82F5B195288

P698

Q34455286-30C9C184-39C0-42E4-B691-719C516AA1E7

P921

Q34455286-04F54896-FF80-46A5-BC3A-E4D31DCEB6BC

P356

P1433

P1476

Interfaces and the driving force of hydrophobic assembly.

@en

P2093

David Chandler

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

P2860

Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects

Interfacial free energy and the hydrophobic effect.

Drying-induced hydrophobic polymer collapse.

Molecular segregation observed in a concentrated alcohol-water solution.

The hydrophobic effect and the organization of living matter.

How protein chemists learned about the hydrophobic factor.

Connecting local structure to interface formation: a molecular scale van der Waals theory of nonuniform liquids.

Hydrophobicity of Long Chain n-Alkyl Carboxylic Acids, as Measured by Their Distribution Between Heptane and Aqueous Solutions

Water? What's so special about it?

Quantification of the hydrophobic interaction by simulations of the aggregation of small hydrophobic solutes in water

P2888

P304

640-647

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

P31

scholarly article

P356

10.1038/NATURE04162

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

P407

P433

7059

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

P478

437

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

P577

2005-09-01T00:00:00Z

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

P5875

7571912

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

P6179

1049606315

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

P698

16193038

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

P921