Arginine and Lysine interactions with π residues in metalloproteins

Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) inter...

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Autores principales: Anitha, Parimelzaghan, Sivasakthi, Vaideeswaran, Lavanya, Pandian, Bag, Susmita, Kumar, Kalavathi Murugan, Anbarasu, Anand, Ramaiah, Sudha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2012
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3488845/
https://www.ncbi.nlm.nih.gov/pubmed/23139592
http://dx.doi.org/10.6026/97320630008820
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author Anitha, Parimelzaghan
Sivasakthi, Vaideeswaran
Lavanya, Pandian
Bag, Susmita
Kumar, Kalavathi Murugan
Anbarasu, Anand
Ramaiah, Sudha
author_facet Anitha, Parimelzaghan
Sivasakthi, Vaideeswaran
Lavanya, Pandian
Bag, Susmita
Kumar, Kalavathi Murugan
Anbarasu, Anand
Ramaiah, Sudha
author_sort Anitha, Parimelzaghan
collection PubMed
description Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) interactions with π (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins. These interactions might play an important role in the global conformational stability in metalloproteins. In spite of its lower natural occurrence (1.76%) the number of Trp residues involved in energetically significant interactions is higher in metalloproteins.
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spelling pubmed-34888452012-11-08 Arginine and Lysine interactions with π residues in metalloproteins Anitha, Parimelzaghan Sivasakthi, Vaideeswaran Lavanya, Pandian Bag, Susmita Kumar, Kalavathi Murugan Anbarasu, Anand Ramaiah, Sudha Bioinformation Hypothesis Metalloproteins have many different functions in cells such as enzymes; signal transduction, transport and storage proteins. About one third of all proteins require metals to carry out their functions. In the present study we have analyzed the roles played by Arg and Lys (cationic side chains) interactions with π (Phe, Tyr or Trp) residues and their role in the structural stability of metalloproteins. These interactions might play an important role in the global conformational stability in metalloproteins. In spite of its lower natural occurrence (1.76%) the number of Trp residues involved in energetically significant interactions is higher in metalloproteins. Biomedical Informatics 2012-09-11 /pmc/articles/PMC3488845/ /pubmed/23139592 http://dx.doi.org/10.6026/97320630008820 Text en © 2012 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Anitha, Parimelzaghan
Sivasakthi, Vaideeswaran
Lavanya, Pandian
Bag, Susmita
Kumar, Kalavathi Murugan
Anbarasu, Anand
Ramaiah, Sudha
Arginine and Lysine interactions with π residues in metalloproteins
title Arginine and Lysine interactions with π residues in metalloproteins
title_full Arginine and Lysine interactions with π residues in metalloproteins
title_fullStr Arginine and Lysine interactions with π residues in metalloproteins
title_full_unstemmed Arginine and Lysine interactions with π residues in metalloproteins
title_short Arginine and Lysine interactions with π residues in metalloproteins
title_sort arginine and lysine interactions with π residues in metalloproteins
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3488845/
https://www.ncbi.nlm.nih.gov/pubmed/23139592
http://dx.doi.org/10.6026/97320630008820
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