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De novo heme protein design.

Wang, Jiangyun.

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De novo heme protein design.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	De novo heme protein design./
作者:	Wang, Jiangyun.
面頁冊數:	191 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3821.
Contained By:	Dissertation Abstracts International64-08B.
標題:	Chemistry, Inorganic. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3101990

De novo heme protein design.
Wang, Jiangyun.

De novo heme protein design. - 191 p.

Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3821.

Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.

One fundamental approach to understanding protein folding and function is to design them from scratch, since the most rigorous way to test our understanding of protein is to put these principles together and see if we can design a well-folded and functional protein. Heme is arguably the most versatile prosthetic group in proteins. How the protein scaffold fine-tunes the heme prothetic group to achieve such diversity of functions is still not well understood, and designing minimal heme peptide complex can often provide substantial insight into these issues.Subjects--Topical Terms:

517253
Chemistry, Inorganic.

De novo heme protein design.
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500 $a Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3821.
500 $a Adviser: Kenneth S. Suslick.
502 $a Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003.
520 $a One fundamental approach to understanding protein folding and function is to design them from scratch, since the most rigorous way to test our understanding of protein is to put these principles together and see if we can design a well-folded and functional protein. Heme is arguably the most versatile prosthetic group in proteins. How the protein scaffold fine-tunes the heme prothetic group to achieve such diversity of functions is still not well understood, and designing minimal heme peptide complex can often provide substantial insight into these issues.
520 $a Our first step is to construct a library of 15-mer peptides with His ligand in the middle. We observed that heme can induce sizable alpha helix formation (30--40%) for these peptides, and in subsequent 2D NMR study, we found that the a helix is well defined in the center, while the structure is dynamic at the terminus. Furthermore, we found that unnatural solvent such as trifluoroethanol or surface salt bridges can stabilize the helix. The cyclic peptide CoIIIporphyrin complex is not only nearly 90% helical and displays well-defined NMR structure, but also unfolds cooperatively. We have also discovered that the helix is tilted, thus only three residues interact with the heme. By making those residues hydrophobic and the rest hydrophilic, we were able to design a more stable protein.
520 $a 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.
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