Arginine residues at internal positions in a protein are always charged - Wikidata - wikimedia - TriplyDB

Arginine residues at internal positions in a protein are always charged

Arginine residues at internal positions in a protein are always charged

http://www.wikidata.org/entity/Q27675548

about

Ensemble force changes that result from human cardiac myosin mutations and a small-molecule effector Fundamental molecular mechanism for the cellular uptake of guanidinium-rich molecules.Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein Principles of agonist recognition in Cys-loop receptors Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights.What stabilizes close arginine pairing in proteins?Buried lysine, but not arginine, titrates and alters transmembrane helix tilt.Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.Translocation and fidelity of Escherichia coli RNA polymerase Free energetics of arginine permeation into model DMPC lipid bilayers: coupling of effective counterion concentration and lateral bilayer dimensions Constant pH molecular dynamics of proteins in explicit solvent with proton tautomerism.Progress in the prediction of pKa values in proteins Investigating the Proton Donor in the NO Reductase from Paracoccus denitrificans.Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.Tryptophan 207 is crucial to the unique properties of the human voltage-gated proton channel, hHV1.Free energy of translocating an arginine-rich cell-penetrating peptide across a lipid bilayer suggests pore formation.Effect of methylation on the side-chain pKa value of arginine Computational simulation strategies for analysis of multisubunit RNA polymerases.Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins.Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.Development of In Silico Protocols to Predict Structural Insights into the Metabolic Activation Pathways of Xenobiotics.Peptide-Based Molecular Hydrogels as Supramolecular Protein Mimics.Probing arginine side-chains and their dynamics with carbon-detected NMR spectroscopy: application to the 42 kDa human histone deacetylase 8 at high pH.Arginine: Its pKa value revisited.Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence.Long-lasting effects of oxy- and sulfoanalogues of L-arginine on enzyme actions Voltage sensor gating charge transfer in a hERG potassium channel model Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE.The nitric-oxide reductase from Paracoccus denitrificans uses a single specific proton pathway.Functional interactions of voltage sensor charges with an S2 hydrophobic plug in hERG channels.Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices.pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.Guanidinium Group Remains Protonated in a Strongly Basic Arginine Solution.A 13C-detected 15N double-quantum NMR experiment to probe arginine side-chain guanidinium 15Nη chemical shifts.The FtsLB sub-complex of the bacterial divisome is tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions.Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins.Unambiguous Determination of Protein Arginine Ionization States in Solution by NMR Spectroscopy.Isolated complexes of the amino acid arginine with polyether and polyamine macrocycles, the role of proton transfer.

P2860

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P2860

Arginine residues at internal positions in a protein are always charged

http://www.wikidata.org/entity/Q27675548

description

2011 nî lūn-bûn

@nan

2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Arginine residues at internal positions in a protein are always charged

@ast

Arginine residues at internal positions in a protein are always charged

@en

Arginine residues at internal positions in a protein are always charged

@nl

type

label

Arginine residues at internal positions in a protein are always charged

@ast

Arginine residues at internal positions in a protein are always charged

@en

Arginine residues at internal positions in a protein are always charged

@nl

prefLabel

Arginine residues at internal positions in a protein are always charged

@ast

Arginine residues at internal positions in a protein are always charged

@en

Arginine residues at internal positions in a protein are always charged

@nl

P1433

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PNAS.1104808108

P1433

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

P1476

Arginine residues at internal positions in a protein are always charged

@en

P2093

Bertrand García-Moreno

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

Gloria R Sue

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

Jamie L Schlessman

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

Michael J Harms

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

P2860

Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance

Structural changes linked to proton translocation by subunit c of the ATP synthase

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

Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter

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

Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum

Low-barrier hydrogen bond in photoactive yellow protein

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

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18954-9

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scholarly article

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4984117

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10.1073/PNAS.1104808108

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47

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108

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2011-11-22T00:00:00Z

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51796130

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22080604

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3223443

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