Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces. - Wikidata - awgldk - TriplyDB

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

http://www.wikidata.org/entity/Q37351619

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Solid-state NMR studies of metal-free SOD1 fibrillar structures.Using the RosettaSurface algorithm to predict protein structure at mineral surfaces.Solid-state NMR studies of proteins immobilized on inorganic surfaces Solid-state NMR studies of HIV-1 capsid protein assemblies.Differences in Dynamics between Crosslinked and Non-Crosslinked Hyaluronates Measured by using Fast Field-Cycling Relaxometry.Toward a structure determination method for biomineral-associated protein using combined solid- state NMR and computational structure prediction.Theory of stochastic dipolar recoupling in solid-state nuclear magnetic resonance.Solution- and adsorbed-state structural ensembles predicted for the statherin-hydroxyapatite system.Internuclear (31)P-(51)V distance measurements in polyoxoanionic solids using rotational echo adiabatic passage double resonance NMR spectroscopy An in vitro scanning microradiography study of the reduction in hydroxyapatite demineralization rate by statherin-like peptides as a function of increasing N-terminal length.SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.

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Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

http://www.wikidata.org/entity/Q37351619

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on May 2007

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@en

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@nl

type

label

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@en

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@nl

prefLabel

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@en

Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

@nl

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J.PNMRS.2006.11.002

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Progress in Nuclear Magnetic Resonance Spectroscopy

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Solid State NMR Studies of Molecular Recognition at Protein-Mineral Interfaces.

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Gary P Drobny

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Gil Goobes

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Patrick S Stayton

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P2860

The effects of human salivary cystatins and statherin on hydroxyapatite crystallization

Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization

Statherin: a major boundary lubricant of human saliva

Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

Bone recognition mechanism of porcine osteocalcin from crystal structure

Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin

Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva

Protein structure prediction using Rosetta

Structure and dynamics of hydrated statherin on hydroxyapatite as determined by solid-state NMR.

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71-85

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scholarly article

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10.1016/J.PNMRS.2006.11.002

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2-3

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