Chad D Paavola, Age 52Carmel, IN

Chad Paavola Phones & Addresses

Carmel, IN

6024 Arbour Ave, Minneapolis, MN 55436

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

Mountain View, CA

2212 Elmwood Ave, Durham, NC 27707 (919) 401-3933

Woodside, CA

Berkeley, CA

El Cerrito, CA

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Chad D Paavola



Company: Nasa ames research center Jun 2001 to Mar 2012 Position: Research scientist


School / High School: University of California, Berkeley 1993 to 1999 Specialities: Biology





Mentions for Chad D Paavola

Resumes and CV


Chad Paavola Photo 1

Research Fellow

Edina, MN
Nasa Ames Research Center Jun 2001 - Mar 2012
Research Scientist
Eli Lilly and Company Jun 2001 - Mar 2012
Research Fellow
Duke University May 1999 - May 2001
Postdoctoral Associate
University of California, Berkeley 1993 - 1999
Edina High School


Us Patents

Ordered Biological Nanostructures Formed From Chaperonin Polypeptides

US Patent:
7816491, Oct 19, 2010
Nov 8, 2002
Appl. No.:
Jonathan D. Trent - Watsonville CA, US
R. Andrew McMillan - San Francisco CA, US
Hiromi Kagawa - Sunnyvale CA, US
Chad D. Paavola - Mountain View CA, US
The United States of America as represented by the Administrator of the National Aeronautics and Space Administration - Washington DC
International Classification:
C07K 14/00
A61K 38/00
US Classification:
530350, 514 2, 977773
The following application relates to nanotemplates, nanostructures, nanoarrays and nanodevices formed from wild-type and mutated chaperonin polypeptides, methods of producing such compositions, methods of using such compositions and particular chaperonin polypeptides that can be utilized in producing such compositions.

Versatile Platform For Nanotechnology Based On Circular Permutations Of Chaperonin Protein

US Patent:
2006008, Apr 20, 2006
Aug 1, 2005
Appl. No.:
Chad Paavola - Mountain View CA, US
Jonathan Trent - Watsonville CA, US
Suzanne Chan - Oakland CA, US
Yi-Fen Li - Sunnyvale CA, US
R. McMillan - San Francisco CA, US
Hiromi Kagawa - Sunnyvale CA, US
International Classification:
C07K 14/195
C07H 21/04
C12P 21/06
C12N 15/74
C12N 1/21
US Classification:
530350000, 435069100, 435252300, 435320100, 536023700
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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