(Q79214694)

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Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 degrees C

scientific article published on 01 November 1999

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scholarly article

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20 December 2019

Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 degrees C (English)

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20 December 2019

author name string

M Häckel

1

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20 December 2019

H J Hinz

2

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20 December 2019

G R Hedwig

3

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20 December 2019

publication date

1 November 1999

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20 December 2019

Biophysical Chemistry

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20 December 2019

82

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20 December 2019

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20 December 2019

1

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20 December 2019

Protein hydration and unfolding--insights from experimental partial specific volumes and unfolded protein models.

1 reference

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Hydration and partial compressibility of biological compounds

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Volumetric properties of proteins and their analogs in diluted water solutions. 1. Partial volumes of amino acids at 15-55 degrees C

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Partial molar heat capacities and volumes of Gly-X-Gly tripeptides in aqueous solution: model studies for the rationalization of thermodynamic parameters of proteins

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The partial molar heat capacity and volume of the peptide backbone group of proteins in aqueous solution

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An alternative interpretation of the heat capacity changes associated with protein unfolding

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The Dielectric Constant of Water and Debye‐Hückel Limiting Law Slopes

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Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range

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Apparent molar volumes of 1-pentanol in water fromT=298 K toT=413 K atp=0.1 MPa andp=19 MPa

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Partial molar volumes of the amino acid side-chains of proteins in aqueous solution: some comments on their estimation using partial molar volumes of amino acids and small peptides

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Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure

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The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data

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7 January 2021

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Heat capacity and conformation of proteins in the denatured state

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Temperature dependence of partial volumes of proteins

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Volume changes on protein folding.

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Apparent molal volumes and heat capacities of aqueous hydrogen chloride and perchloric acid at 15-55.degree.C

1 reference

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Identifiers

10.1016/S0301-4622(99)00104-0

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17030339%20AND%20SRC:MED&resulttype=core&format=json

20 December 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17030339%20AND%20SRC:MED&resulttype=core&format=json

20 December 2019

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