1H nuclear magnetic relaxation dispersion of Cu,Zn superoxide dismutase in the native and guanidinium-induced unfolded forms

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¹H nuclear magnetic relaxation dispersion of Cu,Zn superoxide dismutase in the native and guanidinium-induced unfolded forms. / Libralesso, Elisa; Nerinovski, Kirill; Parigi, Giacomo; Turano, Paola.

In: Biochemical and Biophysical Research Communications, Vol. 328, No. 2, 11.03.2005, p. 633-639.

Research output: Contribution to journal › Article › peer-review

Author

Libralesso, Elisa ; Nerinovski, Kirill ; Parigi, Giacomo ; Turano, Paola. / ¹H nuclear magnetic relaxation dispersion of Cu,Zn superoxide dismutase in the native and guanidinium-induced unfolded forms. In: Biochemical and Biophysical Research Communications. 2005 ; Vol. 328, No. 2. pp. 633-639.

BibTeX

@article{56d136f8772d41b59ac59de3b3b00d27,

title = "1H nuclear magnetic relaxation dispersion of Cu,Zn superoxide dismutase in the native and guanidinium-induced unfolded forms",

abstract = "Potentialities and limitations of the use of 1H NMRD technique for the characterization of the hydration properties of unfolded or partially folded states of proteins are discussed. The copper(I) form of monomeric Cu,Zn superoxide dismutase in its folded state and in the presence of 4 M guanidinium chloride is taken as case system. The dispersion profile, analyzed with an extended relaxation matrix analysis, indicates the presence of long-lived water molecules in the folded state. The observed increase in relaxation at high field upon addition of guanidinium chloride indicates an increase in the number of solvation protons interacting with the protein and exchanging with a time shorter than the protein reorientational time. The observed effect is consistent with an exposed protein surface of SOD in the presence of 4 M guanidinium chloride smaller than what could be expected for a random coil.",

keywords = "Hydration, NMRD, Relaxometry, SOD, Unfolded proteins",

author = "Elisa Libralesso and Kirill Nerinovski and Giacomo Parigi and Paola Turano",

note = "Funding Information: We are grateful to Ivano Bertini and Claudio Luchinat for extensive discussion, corrections, and improvements of the manuscript. This work was supported by MIUR-FIRB, Italy, and the European Union (contract HPRI-CT-2001-50028). Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

year = "2005",

month = mar,

day = "11",

doi = "10.1016/j.bbrc.2005.01.027",

language = "English",

volume = "328",

pages = "633--639",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "2",

}

RIS

TY - JOUR

T1 - 1H nuclear magnetic relaxation dispersion of Cu,Zn superoxide dismutase in the native and guanidinium-induced unfolded forms

AU - Libralesso, Elisa

AU - Nerinovski, Kirill

AU - Parigi, Giacomo

AU - Turano, Paola

N1 - Funding Information: We are grateful to Ivano Bertini and Claudio Luchinat for extensive discussion, corrections, and improvements of the manuscript. This work was supported by MIUR-FIRB, Italy, and the European Union (contract HPRI-CT-2001-50028). Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2005/3/11

Y1 - 2005/3/11

N2 - Potentialities and limitations of the use of 1H NMRD technique for the characterization of the hydration properties of unfolded or partially folded states of proteins are discussed. The copper(I) form of monomeric Cu,Zn superoxide dismutase in its folded state and in the presence of 4 M guanidinium chloride is taken as case system. The dispersion profile, analyzed with an extended relaxation matrix analysis, indicates the presence of long-lived water molecules in the folded state. The observed increase in relaxation at high field upon addition of guanidinium chloride indicates an increase in the number of solvation protons interacting with the protein and exchanging with a time shorter than the protein reorientational time. The observed effect is consistent with an exposed protein surface of SOD in the presence of 4 M guanidinium chloride smaller than what could be expected for a random coil.

AB - Potentialities and limitations of the use of 1H NMRD technique for the characterization of the hydration properties of unfolded or partially folded states of proteins are discussed. The copper(I) form of monomeric Cu,Zn superoxide dismutase in its folded state and in the presence of 4 M guanidinium chloride is taken as case system. The dispersion profile, analyzed with an extended relaxation matrix analysis, indicates the presence of long-lived water molecules in the folded state. The observed increase in relaxation at high field upon addition of guanidinium chloride indicates an increase in the number of solvation protons interacting with the protein and exchanging with a time shorter than the protein reorientational time. The observed effect is consistent with an exposed protein surface of SOD in the presence of 4 M guanidinium chloride smaller than what could be expected for a random coil.

KW - Hydration

KW - NMRD

KW - Relaxometry

KW - SOD

KW - Unfolded proteins

UR - http://www.scopus.com/inward/record.url?scp=13444269136&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2005.01.027

DO - 10.1016/j.bbrc.2005.01.027

M3 - Article

C2 - 15694395

AN - SCOPUS:13444269136

VL - 328

SP - 633

EP - 639

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -

ID: 73950202