Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry. - Wikidata - wikimedia - TriplyDB

Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.

Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.

http://www.wikidata.org/entity/Q37008149

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Characterizing Protein Structure, Dynamics and Conformation in Lyophilized Solids Mass spectrometric approaches to study protein structure and interactions in lyophilized powders.Facile formation of dynamic hydrogel microspheres for triggered growth factor delivery.On-tissue Direct Monitoring of Global Hydrogen/Deuterium Exchange by MALDI Mass Spectrometry: Tissue Deuterium Exchange Mass Spectrometry (TDXMS).Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS)Photolytic labeling to probe molecular interactions in lyophilized powders.Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping Use of glass transitions in carbohydrate excipient design for lyophilized protein formulations

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P2860

Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.

http://www.wikidata.org/entity/Q37008149

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 03 October 2008

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Protein conformation in amorph ...... change with mass spectrometry.

@en

Protein conformation in amorph ...... change with mass spectrometry.

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type

label

Protein conformation in amorph ...... change with mass spectrometry.

@en

Protein conformation in amorph ...... change with mass spectrometry.

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prefLabel

Protein conformation in amorph ...... change with mass spectrometry.

@en

Protein conformation in amorph ...... change with mass spectrometry.

@nl

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BIOPHYSJ.108.139899

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Biophysical Journal

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Protein conformation in amorph ...... change with mass spectrometry.

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Elizabeth M Topp

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Sandipan Sinha

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Todd D Williams

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Yunsong Li

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P2860

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

Hydrogen exchange mass spectrometry for the analysis of protein dynamics

Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding.

What vibrations tell us about proteins.

Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry.

Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state.

Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration.

Trehalose and calcium exert site-specific effects on calmodulin conformation in amorphous solids.

Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry.

Effects of excipients on protein conformation in lyophilized solids by hydrogen/deuterium exchange mass spectrometry.

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5951-5961

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scholarly article

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10.1529/BIOPHYSJ.108.139899

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12

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2008-10-03T00:00:00Z

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18835903

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