Charges in the hydrophobic interior of proteins. - Wikidata - awgldk - TriplyDB

Charges in the hydrophobic interior of proteins.

Charges in the hydrophobic interior of proteins.

http://www.wikidata.org/entity/Q34136707

about

Biomolecular electrostatics and solvation: a computational perspective Design of a switchable eliminase A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches Arginine residues at internal positions in a protein are always charged Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein Proteome adaptation to high temperatures in the ectothermic hydrothermal vent Pompeii worm Conformational Dynamics and Binding Free Energies of Inhibitors of BACE-1: From the Perspective of Protonation Equilibria pH replica-exchange method based on discrete protonation states Bayesian model aggregation for ensemble-based estimates of protein pKa values.Protein dielectric constants determined from NMR chemical shift perturbations Frequent side chain methyl carbon-oxygen hydrogen bonding in proteins revealed by computational and stereochemical analysis of neutron structures.Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.Protein apparent dielectric constant and its temperature dependence from remote chemical shift effects.MTH1 Substrate Recognition--An Example of Specific Promiscuity.High-pressure SAXS study of folded and unfolded ensembles of proteins A simple model for electrical charge in globular macromolecules and linear polyelectrolytes in solution.Constant pH Molecular Dynamics in Explicit Solvent with Enveloping Distribution Sampling and Hamiltonian Exchange How many ionizable groups can sit on a protein hydrophobic core?Molecular simulation of water and hydration effects in different environments: challenges and developments for DFTB based models Photoswitchable red fluorescent protein with a large Stokes shift Large shifts in pKa values of lysine residues buried inside a protein.Proton storage site in bacteriorhodopsin: new insights from quantum mechanics/molecular mechanics simulations of microscopic pK(a) and infrared spectra On the development of protein pKa calculation algorithms.Predicting extreme pKa shifts in staphylococcal nuclease mutants with constant pH molecular dynamics Developing hybrid approaches to predict pKa values of ionizable groups Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation Progress in the prediction of pKa values in proteins Evolutionary, Comparative and Functional Analyses of the Brassinosteroid Receptor Gene, BRI1, in Wheat and Its Relation to Other Plant Genomes Calculation of pK(a) in proteins with the microenvironment modulated-screened coulomb potential Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.Conformational relaxation and water penetration coupled to ionization of internal groups in proteins.A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid β (1-40).Molecular Dynamics Driven Design of pH-Stabilized Mutants of MNEI, a Sweet Protein H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations Rapid calculation of protein pKa values using Rosetta.Functional tuning of the catalytic residue pKa in a de novo designed esterase.Protons as second messenger regulators of G protein signaling.Photoinduced Electron Transfer Elicits a Change in the Static Dielectric Constant of a de Novo Designed Protein.Continuum Electrostatics Approaches to Calculating pKas and Ems in Proteins.The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins.

P2860

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P2860

Charges in the hydrophobic interior of proteins.

http://www.wikidata.org/entity/Q34136707

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Charges in the hydrophobic interior of proteins.

@ast

Charges in the hydrophobic interior of proteins.

@en

Charges in the hydrophobic interior of proteins.

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type

label

Charges in the hydrophobic interior of proteins.

@ast

Charges in the hydrophobic interior of proteins.

@en

Charges in the hydrophobic interior of proteins.

@nl

prefLabel

Charges in the hydrophobic interior of proteins.

@ast

Charges in the hydrophobic interior of proteins.

@en

Charges in the hydrophobic interior of proteins.

@nl

P1433

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P2860

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P356

PNAS.1004213107

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Charges in the hydrophobic interior of proteins.

@en

P2093

Bertrand García-Moreno E

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

Brian R Cannon

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

Carlos A Castañeda

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

Daniel G Isom

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

Priya D Velu

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

P2860

The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

X-ray structure of a voltage-dependent K+ channel

Protein stability promotes evolvability

High Apparent Dielectric Constant Inside a Protein Reflects Structural Reorganization Coupled to the Ionization of an Internal Asp

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme

Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable Groups

A buried lysine that titrates with a normal pKa: Role of conformational flexibility at the protein-water interface as a determinant of pKavalues

In a staphylococcal nuclease mutant the side-chain of a lysine replacing valine 66 is fully buried in the hydrophobic core

The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors

Molecular determinants of the pKa values of Asp and Glu residues in staphylococcal nuclease

P304

16096-16100

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scholarly article

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10.1073/PNAS.1004213107

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P433

37

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107

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2010-08-26T00:00:00Z

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46009564

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20798341

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2941338

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