Light scattering study of human serum albumin in pre-denaturation: relation to dynamic transition in water at 42°C

Vitaliy Bardik; Vladimir Gotsulskii; Evgen Pavlov; Nikolai Malomuzh; Dmitry Nerukh; Igor Yanchuk; Serhiy Lavoryk

doi:10.1016/j.molliq.2012.09.012

Light scattering study of human serum albumin in pre-denaturation: relation to dynamic transition in water at 42°C

Vitaliy Bardik^*, Vladimir Gotsulskii, Evgen Pavlov, Nikolai Malomuzh, Dmitry Nerukh, Igor Yanchuk, Serhiy Lavoryk

^*Corresponding author for this work

Aston University

Research output: Contribution to journal › Special issue › peer-review

Abstract

Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.

Original language	English
Pages (from-to)	60-64
Number of pages	5
Journal	Journal of Molecular Liquids
Volume	176
Early online date	26 Sept 2012
DOIs	https://doi.org/10.1016/j.molliq.2012.09.012
Publication status	Published - Dec 2012
Event	EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011 - , United Kingdom Duration: 11 Sept 2011 → 15 Nov 2011

Bibliographical note

Selected Papers on Molecular Liquids presented at the EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011

Keywords

conformational dynamics
dynamic light scattering
human serum albumin
hydrodynamic radius
hydrogen bonds

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10.1016/j.molliq.2012.09.012

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title = "Light scattering study of human serum albumin in pre-denaturation: relation to dynamic transition in water at 42°C",

abstract = "Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.",

keywords = "conformational dynamics, dynamic light scattering, human serum albumin, hydrodynamic radius, hydrogen bonds",

author = "Vitaliy Bardik and Vladimir Gotsulskii and Evgen Pavlov and Nikolai Malomuzh and Dmitry Nerukh and Igor Yanchuk and Serhiy Lavoryk",

note = "Selected Papers on Molecular Liquids presented at the EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011; EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011 ; Conference date: 11-09-2011 Through 15-11-2011",

year = "2012",

month = dec,

doi = "10.1016/j.molliq.2012.09.012",

language = "English",

volume = "176",

pages = "60--64",

journal = "Journal of Molecular Liquids",

issn = "0167-7322",

publisher = "Elsevier",

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TY - JOUR

T1 - Light scattering study of human serum albumin in pre-denaturation

T2 - EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011

AU - Bardik, Vitaliy

AU - Gotsulskii, Vladimir

AU - Pavlov, Evgen

AU - Malomuzh, Nikolai

AU - Nerukh, Dmitry

AU - Yanchuk, Igor

AU - Lavoryk, Serhiy

N1 - Selected Papers on Molecular Liquids presented at the EMLG/JMLG 2011 Annual Meeting 11 - 15 September 2011

PY - 2012/12

Y1 - 2012/12

N2 - Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.

AB - Protein functional motions are ultimately connected to water dynamics. The goal of this study is to link the conformational dynamics of albumin to a dynamic transition taking place at ∼ 42°C in water. We report the results of dynamic light scattering measurements of albumin aqueous solution in the temperature interval 20-65°C. The processing of the experimental data produced the temperature dependence of the macromolecular hydrodynamic radius. We demonstrate that the growth of the macromolecular size in this temperature range can be divided into two stages that are connected to the dynamical properties of water.

KW - conformational dynamics

KW - dynamic light scattering

KW - human serum albumin

KW - hydrodynamic radius

KW - hydrogen bonds

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U2 - 10.1016/j.molliq.2012.09.012

DO - 10.1016/j.molliq.2012.09.012

M3 - Special issue

AN - SCOPUS:84870477596

SN - 0167-7322

VL - 176

SP - 60

EP - 64

JO - Journal of Molecular Liquids

JF - Journal of Molecular Liquids

Y2 - 11 September 2011 through 15 November 2011

ER -

Light scattering study of human serum albumin in pre-denaturation: relation to dynamic transition in water at 42°C

Abstract

Bibliographical note

Keywords

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