User:Pedrobeltrao/Notebook/Structural analysis of phosphorylation sites

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|style="background-color: #EEE"|[[Image:owwnotebook_icon.png|128px]]<span style="font-size:22px;"> Structural analysis of phosphorylation sites</span>
|style="background-color: #EEE"|[[Image:owwnotebook_icon.png|128px]]<span style="font-size:22px;"> Structural analysis of phosphorylation sites</span>
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==Entry title==
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==Introduction==
The main objective of this study is to try to find systematic ways to study how phosphorylation might regulate proteins based on the analysis of their structures/domains. Only 15% of the known phosphorylation sites of S. cerevisiae map to known folded domains but we can try to find how these generally regulate domain activity, interfaces and how are they conserved in 3D space instead of sequence space.
The main objective of this study is to try to find systematic ways to study how phosphorylation might regulate proteins based on the analysis of their structures/domains. Only 15% of the known phosphorylation sites of S. cerevisiae map to known folded domains but we can try to find how these generally regulate domain activity, interfaces and how are they conserved in 3D space instead of sequence space.

Revision as of 11:49, 15 September 2009

Structural analysis of phosphorylation sites

Introduction

The main objective of this study is to try to find systematic ways to study how phosphorylation might regulate proteins based on the analysis of their structures/domains. Only 15% of the known phosphorylation sites of S. cerevisiae map to known folded domains but we can try to find how these generally regulate domain activity, interfaces and how are they conserved in 3D space instead of sequence space.

  • Data collection and mapping to known domains and structures
  • Domain based analysis
  • Homology models of S. cerevisiae
  • Conservation studies


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