Effects of End Group Termination on Salting-Out Constants for Triglycine. - Wikidata - awgldk - TriplyDB

Effects of End Group Termination on Salting-Out Constants for Triglycine.

Effects of End Group Termination on Salting-Out Constants for Triglycine.

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Dissecting Hofmeister Effects: Direct Anion-Amide Interactions Are Weaker than Cation-Amide Binding.Molecular Modeling for Protein Aggregation and Formulation Responses of polar organic compounds to different ionic environments in aqueous media are interrelated

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Effects of End Group Termination on Salting-Out Constants for Triglycine.

http://www.wikidata.org/entity/Q37503451

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article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on December 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@en

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@nl

type

label

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@en

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@nl

prefLabel

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@en

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@nl

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Journal of Physical Chemistry Letters

P1476

Effects of End Group Termination on Salting-Out Constants for Triglycine.

@en

P2093

Halil I Okur

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

Jana Hladílková

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

Kelvin B Rembert

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

Paul S Cremer

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

Yadagiri Kurra

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

P2860

Development and testing of a general amber force field

What vibrations tell us about proteins.

Why Hofmeister effects of many salts favor protein folding but not DNA helix formation.

Molecular mechanisms of ion-specific effects on proteins.

Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation.

Effects of Hofmeister anions on the phase transition temperature of elastin-like polypeptides

On the theory of solute solubility in mixed solvents.

Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model

Thermodynamic origin of hofmeister ion effects

Reversal of the hofmeister series: specific ion effects on peptides.

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4069-4073

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scholarly article

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10.1021/JZ4022238

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23

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4

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Pavel Jungwirth

Christian Hilty

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2013-12-01T00:00:00Z

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24466388

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