Chad D Paavola, Age 48Carmel, IN

Chad Paavola Phones & Addresses

Carmel, IN

6024 Arbour Ave, Minneapolis, MN 55436

1140 Tangerine Way, Sunnyvale, CA 94087 (408) 746-0181

1687 Le Roy Ave, Berkeley, CA 94709

El Cerrito, CA

Durham, NC

Woodside, CA

Mountain View, CA

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Chad D Paavola

Linkedin

Work

Company: Eli lilly and company Mar 2012 to Aug 2013 Address: Indianapolis, Indiana Area Position: Research advisor

Education

Degree: Ph. D. School / High School: University of California, Berkeley 1993 to 1999 Specialities: Molecular and Cell Biology

Industries

Research

Mentions for Chad D Paavola

Resumes

Resumes

Chad Paavola Photo 1

Bioproducts Researcher

Position:
Research Advisor at Eli Lilly and Company
Location:
Indianapolis, Indiana
Industry:
Research
Work:
Eli Lilly and Company - Indianapolis, Indiana Area since Mar 2012
Research Advisor
NASA Ames Research Center Jun 2001 - Mar 2012
Research Scientist
Duke University May 1999 - May 2001
Postdoctoral Associate
Education:
University of California, Berkeley 1993 - 1999
Ph. D., Molecular and Cell Biology

Publications

Us Patents

Versatile Platform For Nanotechnology Based On Circular Permutations Of Chaperonin Protein

US Patent:
2006008, Apr 20, 2006
Filed:
Aug 1, 2005
Appl. No.:
11/194991
Inventors:
Chad Paavola - Mountain View CA,
Jonathan Trent - Watsonville CA,
Suzanne Chan - Oakland CA,
Yi-Fen Li - Sunnyvale CA,
R. McMillan - San Francisco CA,
Hiromi Kagawa - Sunnyvale CA,
International Classification:
C07K 14/195
C07H 21/04
C12P 21/06
C12N 15/74
C12N 1/21
US Classification:
530350000, 435069100, 435252300, 435320100, 536023700
Abstract:
The present invention provides chaperonin polypeptides which are modified to include N-terminal and C-terminal ends that are relocated from the central pore region to various different positions in the polypeptide which are located on the exterior of the folded modified chaperonin polypeptide. In the modified chaperonin polypeptide, the naturally-occurring N-terminal and C-terminal ends are joined together directly or with an intervening linker peptide sequence. The relocated N-terminal or C-terminal ends can be covalently joined to, or bound with another molecule such as a nucleic acid molecule, a lipid, a carbohydrate, a second polypeptide, or a nanoparticle. The modified chaperonin polypeptides can assemble into double-ringed chaperonin structures. Further, the chaperonin structures can organize into higher order structures such as nanofilaments or nanoarrays which can be used to produce nanodevices and nanocoatings.

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