A buried lysine that titrates with a normal pKa: Role of conformational flexibility at the protein-water interface as a determinant of pKavalues - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q27650168

about

Biomolecular electrostatics and solvation: a computational perspective The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors Arginine residues at internal positions in a protein are always charged Bayesian model aggregation for ensemble-based estimates of protein pKa values.Novel covalent bond in proteins: calculations on model systems question the bond stability.Translocation and fidelity of Escherichia coli RNA polymerase Structural origins of high apparent dielectric constants experienced by ionizable groups in the hydrophobic core of a protein Charges in the hydrophobic interior of proteins.Large shifts in pKa values of lysine residues buried inside a protein.Geometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5'-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.Developing hybrid approaches to predict pKa values of ionizable groups Progress in the prediction of pKa values in proteins Conformational consequences of ionization of Lys, Asp, and Glu buried at position 66 in staphylococcal nuclease 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.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.Breaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum.Progress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energies Arginine side chain interactions and the role of arginine as a gating charge carrier in voltage sensitive ion channels.Estimating the pKa values of basic and acidic side chains in ion channels using electrophysiological recordings: a robust approach to an elusive problem.Quantum cluster size and solvent polarity effects on the geometries and Mössbauer properties of the active site model for ribonucleotide reductase intermediate X: a density functional theory study.DFT calculations of comparative energetics and ENDOR/Mössbauer properties for two protonation states of the iron dimer cluster of ribonucleotide reductase intermediate X.pKa predictions with a coupled finite difference Poisson-Boltzmann and Debye-Hückel method.DFT calculations for intermediate and active states of the diiron center with a tryptophan or tyrosine radical in Escherichia coli ribonucleotide reductase Influence of glutamic acid residues and pH on the properties of transmembrane helices.Microscopic mechanisms that govern the titration response and pKa values of buried residues in staphylococcal nuclease mutants.Exploring conformational changes coupled to ionization states using a hybrid Rosetta-MCCE protocol.Blind, one-eyed, or eagle-eyed? pKa calculations during blind predictions with staphylococcal nuclease.MCCE analysis of the pKas of introduced buried acids and bases in staphylococcal nuclease.Toward accurate prediction of pKa values for internal protein residues: the importance of conformational relaxation and desolvation energy.Electrostatic pKa computations in proteins: role of internal cavities.Site-specific amino acid substitution in dodecameric peptides determines the stability and unfolding of c-MYC quadruplex promoting apoptosis in cancer cells

P2860

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P2860

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

http://www.wikidata.org/entity/Q27650168

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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A buried lysine that titrates ...... as a determinant of pKavalues

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Protein Science

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A buried lysine that titrates ...... as a determinant of pKavalues

@en

P2093

Ana Damjanović

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

Bertrand García-Moreno

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

Gloria R Sue

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

Jamie L Schlessman

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Michael J Harms

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

Michael S Chimenti

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability

Buried charged surface in proteins

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

The crystal structure of staphylococcal nuclease refined at 1.7 A resolution

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

The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 A

Solution structures of staphylococcal nuclease from multidimensional, multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and thymidine-3',5'-bisphosphate

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

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833-45

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scholarly article

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10.1110/PS.073397708

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5

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17

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2008-05-01T00:00:00Z

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5483732

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18369193

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2327280

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