Biological water

Its vital role in macromolecular structure and function.

Florin Despa

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Water in tissues and cells is confined by intervening cellular components and is subject to structural effects that are not present in its bulk counterpart. The structuring effects lower the dielectric susceptibility of water molecules and induce a "red shift" of their relaxation frequency. This is also a source of polarization fields that contribute to the effective interactions between macromolecules. The behavior of water molecules at hydrophilic sites is different from that at hydrophobic sites, and this dissimilar behavior promotes the anisotropy of the hydration shell of proteins. The anisotropy of the hydration shell is essential for the enzyme function, but it is also important in detecting denaturation of the protein (i.e., proteins expose their hydrophobic parts to water during unfolding). The most significant differences between biological and ordinary water will be presented along with how this information can be used to decipher patterns in dynamical behavior of biological water and to detect possible structural changes of the cellular components.

Original languageEnglish (US)
Pages (from-to)1-11
Number of pages11
JournalAnnals of the New York Academy of Sciences
Volume1066
DOIs
StatePublished - Dec 2005
Externally publishedYes

Fingerprint

Water
Anisotropy
Hydration
Protein Denaturation
Proteins
Denaturation
Molecules
Macromolecules
Polarization
Tissue
Enzymes
Protein
Shell

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Biological water : Its vital role in macromolecular structure and function. / Despa, Florin.

In: Annals of the New York Academy of Sciences, Vol. 1066, 12.2005, p. 1-11.

Research output: Contribution to journalArticle

@article{3f89ffdba2a94838b509ae1baeb8c78b,
title = "Biological water: Its vital role in macromolecular structure and function.",
abstract = "Water in tissues and cells is confined by intervening cellular components and is subject to structural effects that are not present in its bulk counterpart. The structuring effects lower the dielectric susceptibility of water molecules and induce a {"}red shift{"} of their relaxation frequency. This is also a source of polarization fields that contribute to the effective interactions between macromolecules. The behavior of water molecules at hydrophilic sites is different from that at hydrophobic sites, and this dissimilar behavior promotes the anisotropy of the hydration shell of proteins. The anisotropy of the hydration shell is essential for the enzyme function, but it is also important in detecting denaturation of the protein (i.e., proteins expose their hydrophobic parts to water during unfolding). The most significant differences between biological and ordinary water will be presented along with how this information can be used to decipher patterns in dynamical behavior of biological water and to detect possible structural changes of the cellular components.",
author = "Florin Despa",
year = "2005",
month = "12",
doi = "10.1196/annals.1363.023",
language = "English (US)",
volume = "1066",
pages = "1--11",
journal = "Annals of the New York Academy of Sciences",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Biological water

T2 - Its vital role in macromolecular structure and function.

AU - Despa, Florin

PY - 2005/12

Y1 - 2005/12

N2 - Water in tissues and cells is confined by intervening cellular components and is subject to structural effects that are not present in its bulk counterpart. The structuring effects lower the dielectric susceptibility of water molecules and induce a "red shift" of their relaxation frequency. This is also a source of polarization fields that contribute to the effective interactions between macromolecules. The behavior of water molecules at hydrophilic sites is different from that at hydrophobic sites, and this dissimilar behavior promotes the anisotropy of the hydration shell of proteins. The anisotropy of the hydration shell is essential for the enzyme function, but it is also important in detecting denaturation of the protein (i.e., proteins expose their hydrophobic parts to water during unfolding). The most significant differences between biological and ordinary water will be presented along with how this information can be used to decipher patterns in dynamical behavior of biological water and to detect possible structural changes of the cellular components.

AB - Water in tissues and cells is confined by intervening cellular components and is subject to structural effects that are not present in its bulk counterpart. The structuring effects lower the dielectric susceptibility of water molecules and induce a "red shift" of their relaxation frequency. This is also a source of polarization fields that contribute to the effective interactions between macromolecules. The behavior of water molecules at hydrophilic sites is different from that at hydrophobic sites, and this dissimilar behavior promotes the anisotropy of the hydration shell of proteins. The anisotropy of the hydration shell is essential for the enzyme function, but it is also important in detecting denaturation of the protein (i.e., proteins expose their hydrophobic parts to water during unfolding). The most significant differences between biological and ordinary water will be presented along with how this information can be used to decipher patterns in dynamical behavior of biological water and to detect possible structural changes of the cellular components.

UR - http://www.scopus.com/inward/record.url?scp=33749046358&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749046358&partnerID=8YFLogxK

U2 - 10.1196/annals.1363.023

DO - 10.1196/annals.1363.023

M3 - Article

VL - 1066

SP - 1

EP - 11

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

SN - 0077-8923

ER -