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University of Illinois at Urbana-Champaign

De Novo Heme Protein Design

Abstract

dc:description

"We have developed an interesting hypothesis for Olfactory Receptor (OR) mechanism. We are so sensitive to thiols and amines that the most natural way to explain this is that OR is a metalloprotein. We have found a consensus sequence ""HXXCE"" in the 4--5 loop of ORs, which not only binds strongly to Cu2+ and Zn2+, but also turns alpha helical after metal binding. Since the 4--5 loop is as hydrophobic as the fourth helix of OR, charge neutralization of metal ion increases its hydrophobicity, thus it might turn into transmembrane helix and replace the fourth helix. Endogenous ligand binding to the metal site might disturb the charge balance and triggers helix motion, which results in a cell signaling cascade, and eventually the sense of smell."

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Chemistry
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Wang, Jiangyun
Contributors dc:contributor
  • Kenneth S. Suslick

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3101990
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/84121

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Wang, Jiangyun. De Novo Heme Protein Design. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/84121