P
Pedro M. Nieto
Researcher at University of Seville
Publications - 107
Citations - 3929
Pedro M. Nieto is an academic researcher from University of Seville. The author has contributed to research in topics: Nuclear magnetic resonance spectroscopy & Chondroitin sulfate. The author has an hindex of 33, co-authored 103 publications receiving 3700 citations. Previous affiliations of Pedro M. Nieto include Autonomous University of Madrid & University of Barcelona.
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Carbon-13 NMR chemical shifts. A single rule to determine the conformation of calix[4]arenes
TL;DR: The conformations of calix [4] arenes can be deduced from the 13 C NMR chemical shift of the methylene groups connecting each pair of aromatic rings.
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Tachykinins and Tachykinin Receptors: Structure and Activity Relationships
Teresa A. Almeida,Javier Rojo,Pedro M. Nieto,Francisco M. Pinto,Mariano Hernández,Julio D. Martín,M.L. Candenas +6 more
TL;DR: The major aim of the present article is to review the structure-activity data that exist for tachykinins and their receptors, with the purpose of getting insight into basic structural requirements that determine ligand/receptor interaction.
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Ligand–Receptor Binding Affinities from Saturation Transfer Difference (STD) NMR Spectroscopy: The Binding Isotherm of STD Initial Growth Rates
TL;DR: It is demonstrated that the effects of these factors are cancelled out by analyzing the protein-ligand association curve using STD values at the limit of zero saturation time, when virtually no ligand rebinding or relaxation takes place.
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STD-NMR: application to transient interactions between biomolecules—a quantitative approach
Jesús Angulo,Pedro M. Nieto +1 more
TL;DR: The objective of this article is to review the current status of this powerful NMR technique, with particular emphasis on quantitative applications, within the framework of the (bio-)chemistry of molecular recognition.
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Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.
Juan Luis Asensio,Francisco Javier Cañada,Hans-Christian Siebert,José Laynez,Ana Poveda,Pedro M. Nieto,UM Soedjanaamadja,Hans-Joachim Gabius,Jesús Jiménez-Barbero +8 more
TL;DR: The resulting model conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought.