Title |
Mapping the amino acid properties of constituent nucleoporins onto the yeast nuclear pore complex |
Authors |
Ashok Kunda1,#, Narayanan H Krishnan1,# & VV Krishnan2,3,* |
Affiliation |
1Davis Senior High School, 315 West 14th Street, Davis, CA 95616; 2Department of Chemistry, California State University, Fresno CA 93740 and; 3Department of Medical Pathology and Laboratory Medicine, University of California Davis School of Medicine, Davis, CA 95616
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krish@csufresno.edu; vvkrishnan@ucdavis.edu; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received November 26, 2013; Revised January 04, 2014; Accepted January 06, 2014; Published February 19, 2014
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Abstract |
Visualization of molecular structures aids in the understanding of structural and functional roles of biological macromolecules. Macromolecular transport between the cell nucleus and cytoplasm is facilitated by the nuclear pore complex (NPC). The ring structure of the NPC is large and contains several distinct proteins (nucleoporins) which function as a selective gate for the passage of certain molecules into and out of the nucleus. In this note we demonstrate the utility of a python code that allows direct mapping of the physiochemical properties of the constituent nucleoporins on the scaffold of the yeast NPC’s cytoplasmic view. We expect this tool to be useful for researchers to visualize the NPC based on their physiochemical properties and how it alters when specific mutations are introduced in one or more of the nucleoporins. The code developed using Python is available freely from the authors.
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Keywords |
NPC (nuclear pore complex), IDP (intrinsically disordered protein), AA Index
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Citation |
Kunda et al. Bioinformation 10(2): 094-097 (2014)
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Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |