Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein. - Wikidata - wikimedia - TriplyDB

Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.

Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.

http://www.wikidata.org/entity/Q36026100

about

Protein stability: computation, sequence statistics, and new experimental methods Structural and thermodynamic consequences of burial of an artificial ion pair in the hydrophobic interior of a protein Correlation of phenotype/genotype in a cohort of 23 xeroderma pigmentosum-variant patients reveals 12 new disease-causing POLH mutations A Virtual Mixture Approach to the Study of Multistate Equilibrium: Application to Constant pH Simulation in Explicit Water Buried ionizable networks are an ancient hallmark of G protein-coupled receptor activation A hydrophobic spine stabilizes a surface-exposed α-helix according to analysis of the solvent-accessible surface area.Computational simulation strategies for analysis of multisubunit RNA polymerases.The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins.Measuring the successes and deficiencies of constant pH molecular dynamics: a blind prediction study.Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications.Prominent features of the amino acid mutation landscape in cancer.Uncovering pH-dependent transient states of proteins with buried ionizable residues.Microscopic mechanisms that govern the titration response and pKa values of buried residues in staphylococcal nuclease mutants.

P2860

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P2860

Structural reorganization triggered by charging of Lys residues in the hydrophobic interior of a protein.

http://www.wikidata.org/entity/Q36026100

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Structural reorganization trig ...... ophobic interior of a protein.

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Structural reorganization trig ...... ophobic interior of a protein.

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type

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Structural reorganization trig ...... ophobic interior of a protein.

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Structural reorganization trig ...... ophobic interior of a protein.

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Structural reorganization trig ...... ophobic interior of a protein.

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Structural reorganization trig ...... ophobic interior of a protein.

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J.STR.2012.03.023

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Structural reorganization trig ...... ophobic interior of a protein.

@en

P2093

Aaron C Robinson

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

Ananya Majumdar

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

Annie Heroux

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

Bertrand García-Moreno

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

Jamie L Schlessman

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

Michael S Chimenti

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

Victor S Khangulov

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

P2860

Mobile unnatural amino acid side chains in the core of staphylococcal nuclease

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

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

Arginine residues at internal positions in a protein are always charged

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1071-1085

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scholarly article

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10.1016/J.STR.2012.03.023

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6

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2012-05-25T00:00:00Z

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