Tendamistat surface accessibility to the TEMPOL paramagnetic probe

Maria Scarselli, Andrea Bernini, Claudia Segoni, Henriette Molinari, Gennaro Esposito, Arthur M. Lesk, Franco Laschi, Pierandrea Temussi, Neri Niccolai

Research output: Contribution to journalArticle

Abstract

TEMPOL, the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl, has been used to determine the surface characteristics of tendamistat, a small protein with a well-characterised structure both in solution and in the crystal. A good correlation has been found between predicted regions of exposed protein surface and the intensity attenuations induced by the probe on 2D NMR TOCSY cross peaks of tendamistat in the paramagnetic water solution. All the high paramagnetic effects have been interpreted in terms of more efficient competition of TEMPOL with water molecules at some surface positions. The active site of tendamistat coincides with the largest surface patch accessible to the probe. A strong hydration of protein N and C termini can also be suggested by this structural approach, as these locations exhibit reduced paramagnetic pertubations. Provided that the solution structure is known, the use of this paramagnetic probe seems to be well suited to delineate the dynamic behaviour of the protein surface and, more generally, to gain relevant information about the molecular presentation processes.

Original languageEnglish (US)
Pages (from-to)125-133
Number of pages9
JournalJournal of Biomolecular NMR
Volume15
Issue number2
DOIs
StatePublished - Dec 1 1999

Fingerprint

Membrane Proteins
Spin Labels
Water
Protein C
Hydration
Catalytic Domain
Proteins
Nuclear magnetic resonance
Crystals
Molecules
tendamistate
2,2,6,6-tetramethyl-1-piperidine

Keywords

  • Molecular presentation
  • Protein structure
  • Spin-labels
  • Surface accessibility
  • Tendamistat

ASJC Scopus subject areas

  • Spectroscopy
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Scarselli, M., Bernini, A., Segoni, C., Molinari, H., Esposito, G., Lesk, A. M., ... Niccolai, N. (1999). Tendamistat surface accessibility to the TEMPOL paramagnetic probe. Journal of Biomolecular NMR, 15(2), 125-133. https://doi.org/10.1023/A:1008319507565

Tendamistat surface accessibility to the TEMPOL paramagnetic probe. / Scarselli, Maria; Bernini, Andrea; Segoni, Claudia; Molinari, Henriette; Esposito, Gennaro; Lesk, Arthur M.; Laschi, Franco; Temussi, Pierandrea; Niccolai, Neri.

In: Journal of Biomolecular NMR, Vol. 15, No. 2, 01.12.1999, p. 125-133.

Research output: Contribution to journalArticle

Scarselli, M, Bernini, A, Segoni, C, Molinari, H, Esposito, G, Lesk, AM, Laschi, F, Temussi, P & Niccolai, N 1999, 'Tendamistat surface accessibility to the TEMPOL paramagnetic probe', Journal of Biomolecular NMR, vol. 15, no. 2, pp. 125-133. https://doi.org/10.1023/A:1008319507565
Scarselli, Maria ; Bernini, Andrea ; Segoni, Claudia ; Molinari, Henriette ; Esposito, Gennaro ; Lesk, Arthur M. ; Laschi, Franco ; Temussi, Pierandrea ; Niccolai, Neri. / Tendamistat surface accessibility to the TEMPOL paramagnetic probe. In: Journal of Biomolecular NMR. 1999 ; Vol. 15, No. 2. pp. 125-133.
@article{5e2a613e678b440d8a4440323ae48f40,
title = "Tendamistat surface accessibility to the TEMPOL paramagnetic probe",
abstract = "TEMPOL, the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl, has been used to determine the surface characteristics of tendamistat, a small protein with a well-characterised structure both in solution and in the crystal. A good correlation has been found between predicted regions of exposed protein surface and the intensity attenuations induced by the probe on 2D NMR TOCSY cross peaks of tendamistat in the paramagnetic water solution. All the high paramagnetic effects have been interpreted in terms of more efficient competition of TEMPOL with water molecules at some surface positions. The active site of tendamistat coincides with the largest surface patch accessible to the probe. A strong hydration of protein N and C termini can also be suggested by this structural approach, as these locations exhibit reduced paramagnetic pertubations. Provided that the solution structure is known, the use of this paramagnetic probe seems to be well suited to delineate the dynamic behaviour of the protein surface and, more generally, to gain relevant information about the molecular presentation processes.",
keywords = "Molecular presentation, Protein structure, Spin-labels, Surface accessibility, Tendamistat",
author = "Maria Scarselli and Andrea Bernini and Claudia Segoni and Henriette Molinari and Gennaro Esposito and Lesk, {Arthur M.} and Franco Laschi and Pierandrea Temussi and Neri Niccolai",
year = "1999",
month = "12",
day = "1",
doi = "10.1023/A:1008319507565",
language = "English (US)",
volume = "15",
pages = "125--133",
journal = "Journal of Biomolecular NMR",
issn = "0925-2738",
publisher = "Springer Netherlands",
number = "2",

}

TY - JOUR

T1 - Tendamistat surface accessibility to the TEMPOL paramagnetic probe

AU - Scarselli, Maria

AU - Bernini, Andrea

AU - Segoni, Claudia

AU - Molinari, Henriette

AU - Esposito, Gennaro

AU - Lesk, Arthur M.

AU - Laschi, Franco

AU - Temussi, Pierandrea

AU - Niccolai, Neri

PY - 1999/12/1

Y1 - 1999/12/1

N2 - TEMPOL, the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl, has been used to determine the surface characteristics of tendamistat, a small protein with a well-characterised structure both in solution and in the crystal. A good correlation has been found between predicted regions of exposed protein surface and the intensity attenuations induced by the probe on 2D NMR TOCSY cross peaks of tendamistat in the paramagnetic water solution. All the high paramagnetic effects have been interpreted in terms of more efficient competition of TEMPOL with water molecules at some surface positions. The active site of tendamistat coincides with the largest surface patch accessible to the probe. A strong hydration of protein N and C termini can also be suggested by this structural approach, as these locations exhibit reduced paramagnetic pertubations. Provided that the solution structure is known, the use of this paramagnetic probe seems to be well suited to delineate the dynamic behaviour of the protein surface and, more generally, to gain relevant information about the molecular presentation processes.

AB - TEMPOL, the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl, has been used to determine the surface characteristics of tendamistat, a small protein with a well-characterised structure both in solution and in the crystal. A good correlation has been found between predicted regions of exposed protein surface and the intensity attenuations induced by the probe on 2D NMR TOCSY cross peaks of tendamistat in the paramagnetic water solution. All the high paramagnetic effects have been interpreted in terms of more efficient competition of TEMPOL with water molecules at some surface positions. The active site of tendamistat coincides with the largest surface patch accessible to the probe. A strong hydration of protein N and C termini can also be suggested by this structural approach, as these locations exhibit reduced paramagnetic pertubations. Provided that the solution structure is known, the use of this paramagnetic probe seems to be well suited to delineate the dynamic behaviour of the protein surface and, more generally, to gain relevant information about the molecular presentation processes.

KW - Molecular presentation

KW - Protein structure

KW - Spin-labels

KW - Surface accessibility

KW - Tendamistat

UR - http://www.scopus.com/inward/record.url?scp=0032695225&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032695225&partnerID=8YFLogxK

U2 - 10.1023/A:1008319507565

DO - 10.1023/A:1008319507565

M3 - Article

C2 - 10605086

AN - SCOPUS:0032695225

VL - 15

SP - 125

EP - 133

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

SN - 0925-2738

IS - 2

ER -