Proteopedia - User contributions [en]

Group:SMART:Teams

2009-04-26T22:30:43Z

David Stack:

=Overview of the Program=
[[Image:SMART Teams photo 1.jpg|left]]
[[Image:Smart Teams photo 5.jpg|right|200px]]

What do you get when you combine enthusiastic high school teachers and their students, scientists excited about their research, and Rapid Prototyping technology? SMART (Students Modeling A Research Topic) Teams! In this multi-faceted program, students develop teamwork as they delve into the molecular world, explore science as a process and not just a collection of facts, and work closely with a researcher to understand and model the structure-function relationship of a protein the researcher studies. After designing and building a model of the protein using Rapid Prototyping technology, SMART teams create an oral presentation explaining their work to a lay audience and a poster which is presented to a scientific audience.

SMART Teams consist of a teacher who has participated in the Center for BioMolecular Modeling's summer course, Modeling the Molecular World, Part I (or its predecessor, Genes, Schemes and Molecular Machines), students, and a research mentor.

{{Clear}}
=Qualification, Research, and Presentation Phases=
Teams work to complete the three phases of the program:
==Qualification Phase==
[[Image:Smart team 2.jpg|left|200px]]

Students review basic concepts of protein structure and are introduced to the use of molecular visualization software (RasMol) to generate virtual images of proteins based on atomic coordinates obtained from the Protein Data Bank. Each Team then demonstrates their knowledge of these topics by designing and building a physical model of a protein that is currently in the news. This phase of the program ends with the Qualification Exam, a friendly yet competitive event in which Teams compete to demonstrate their expertise in all areas related to the physical modeling of molecular structures.

{{Clear}}
==Research and Model Design Phase==
[[Image:Smart Team photo 3.jpg|left|200px]]

Qualified SMART Teams are then matched with a research scientist who is investigating a specific protein in their laboratory. The matching of Teams and mentors is accomplished through a “speed dating” activity in which all the Teams meet all of the potential mentors in a series of intense five-minute conversations. Compatible Teams and mentors are matched following this activity.

Once matched, the Team visits the mentor’s laboratory and learns about their research project. The Team identifies a protein that is the focus of the lab’s research project, and then designs a physical model. During this research and design phase, the Team works closely with the mentor to create a physical model that will be useful as a “thinking tool” in the laboratory.

{{Clear}}
==Presentation Phase==
[[Image:Smart Team photo 4.jpg|left|200px]]

Following the design and construction of the physical model, the Team continues to work with their mentor and teacher to develop a short oral presentation of their work for a lay audience, and a poster that is presented in a poster session within the scientific community. Some teams also present their posters to their local PTA or school board, or at a scientific research meeting, such as ASBMB or ASM.

{{clear}}
=SMART Team Proteopedia Pages=
==Local SMART Teams==
===2008-2009===
[[A_Physical_Model_of_the_β2-Adrenergic_Receptor|A SMART Team Molecular Story - Madison West High School Project of β2-Adrenergic Receptor]]

[[A_Physical_Model_of_the_Structure_of_GNNQQNY_from_Yeast_Prion_Sup35|A SMART Team Molecular Story - Community SMART Team of Southeast Wisconsin Project of GNNQQNY from Yeast Prion Sup35]]
===2009-2010===
==HHMI SMART Teams==
===2008-2009===
===2009-2010===
==Remote SMART Teams==
===2008-2009===
===2009-2010===

Group:SMART:A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35

2009-04-22T19:26:50Z

David Stack: /* Our Poster and Presentations */

=='''A SMART Team Molecular Story --- from the 2009 Community SMART Team of Southeast Wisconsin'''==

:Students -- Moses Misplon, Meghan Murphy, Joel Pollen, Christine Pollnow, Maia Stack

:Advisor: David Stack, Ph.D., University of Wisconsin–Milwaukee

:Mentor: Anita Manogaran, Ph.D., University of Illinois at Chicago
<applet load='1yjp_our_version' size='300' frame='true' align='right' caption='GNNQQNY - a section of the [PSI+] prion' scene='User:David_Stack/Workbench/Movie_companion/3' />

<swf> http://myweb.msoe.edu/~hoelzer/Community%202008-2009.swf</swf>

{{clear}}

==Abstract for Our Project==

Fatal prion diseases, such as Creutzfeldt-Jakob disease in humans, are associated with the conversion of the normally folded mammalian PrP protein to a misfolded prion form that aggregates. Understanding how prions behave has been greatly facilitated by the study of prions in Saccharomyces cerevisiae, or baker’s yeast. In yeast, the translation release factor, Sup35, misfolds to form the [PSI+] prion. Although the Sup35 protein has a significantly different primary sequence from PrP, its prion form behaves similarly to human prions. The N-terminus of Sup35 is Q/N-rich and responsible for prion formation. Determining the structure of this region has proven difficult since the N-terminus forms aggregates instead of the ordered crystals required for structural studies. However, a small seven amino acid sequence (GNNQQNY) from Sup35's N-terminus was crystallized by Nelson et al. (2005). We have constructed a 3D physical model of GNNQQNY as part of the MSOE SMART Teams program using 3D printing technology. GNNQQNY's structure suggests that multiple prion molecules assemble into strong fibrous aggregates through tightly structured interlocking parallel beta sheets called a cross-β spine. The structure of GNNQQNY suggests a potential model of how human prions assemble, which could potentially help in developing therapies that prevent aggregation. Supported by a grant from NIH-NCRR-SEPA.

{{Clear}}

==Creating the Physical Model of GNNQQNY==

<applet load='1yjp.pdb' size='400' frame='true' align='left' caption='Community SMART Team Model - GNNQQNY from Yeast Prion Sup35' scene='User:David_Stack/Workbench/1yjp_our_version/9'/>

Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. To design our model of the structure of the GNNQQNY from yeast prion Sup35, we used the atomic coordinates for this structure as reported in the pdb file 1yjp, from the Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics.

Beginning with <scene name='User:David_Stack/Workbench/Prion_step_one/1'>the raw 1yjp pdb file</scene>, the format was set to ball and stick and the spacefill set to 225. The <scene name='User:David_Stack/Workbench/Prion_step_two/1'>water molecules were deleted </scene> and half the model was <scene name='User:David_Stack/Workbench/Prion_step_three/1'> colored cyan </scene> to represent the wet interface. The dry interface was <scene name='User:David_Stack/Workbench/Prion_step_three_and_a_half/1'> colored blue </scene> and the backbone was <scene name='User:David_Stack/Workbench/Prion_step_four/1'> colored white. </scene> The <scene name='User:David_Stack/Workbench/Prion_step_five/1'> oxygen molecules </scene> were colored red for Asn2 and Asn3, orange for Gln4 and Gln5 and yellow for Asn6 and Tyr7.

A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer.

{{Clear}}

==References==
1) Nelson, R., Sawaya, MR., Balbirnie, M., Madsen, AO., Riekel, C., Grothe, R. & Eisenberg, D. (2005). Structure of the cross ß-spine of amyloid-like fibrils. Nature. 435, 773-778.

2) Shkundina, I.S. & Ter-Avanesyan, M.D. (2007). Prions. Biochemistry (Moscow). 72:13, 1519-1536.

{{Clear}}

==Our Poster and Presentations==
[[Image:CommunitySMARTTeamwithMentor.jpg|Community SMART Team with Mentor| 350px]]
[[Image:2008-09communitysmartteam.jpg|Community SMART Team at Medical College of WI| 350px]]
[[Image:Community_SMART_Team_GNNQQNY.jpg|Community SMART Team Poster| 350px]]

{{Clear}}

Presentations of our project, poster, and physical models:

-- Medical College of Wisconsin SMART Team Poster Session, March 6, 2009

-- American Society for Biochemistry and Molecular Biology Undergraduate Research Poster Competition, April 18, 2009

-- University of Wisconsin Milwaukee Undergraduate Research Symposium, April 24, 2009

{{Clear}}

==MSOE Center for BioMolecular Modeling and SMART Teams==
[[Image:Center for BioMolecular Modeling Logo.jpg|left|200px]]
[[Image:Smart Teams photo 5.jpg|right|120px]]

SMART Teams (Students Modeling A Research Topic) is a science outreach program developed by the MSOE Center for BioMolecular Modeling. In this program, teams of high school students work with a local resarch lab to design and build a physical model of a protein that is being investigated by the lab. The goal of the SMART Team program is to introduce students to the real world of science --- as it exists in a local research lab. The development of this program was supported by grants from the NIH-NCRR SEPA program (Science Education Partnership Award) and an HHMI Precollege Science Education Award. For more information about this program, visit the CBM web site at [http://www.rpc.msoe.edu/cbm www.rpc.msoe.edu/cbm] .

File:2008-09communitysmartteam.jpg

2009-04-22T19:24:56Z

David Stack: 2008-09 Community SMART Team of Southeast Wisconsin at poster session at the Medical College of Wisconsin

== Summary ==
2008-09 Community SMART Team of Southeast Wisconsin at poster session at the Medical College of Wisconsin
== Licensing ==
{{GFDL}}

Group:SMART:A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35

2009-04-09T16:20:32Z

David Stack:

=='''A SMART Team Molecular Story --- from the 2009 Community SMART Team of Southeast Wisconsin'''==

:Students -- Moses Misplon, Meghan Murphy, Joel Pollen, Christine Pollnow, Maia Stack

:Advisor: David Stack, Ph.D., University of Wisconsin–Milwaukee

:Mentor: Anita Manogaran, Ph.D., University of Illinois at Chicago
<applet load='1yjp_our_version' size='300' frame='true' align='right' caption='GNNQQNY - a section of the [PSI+] prion' scene='User:David_Stack/Workbench/Movie_companion/3' />

<swf> http://myweb.msoe.edu/~hoelzer/Community%202008-2009.swf</swf>

{{clear}}

==Abstract for Our Project==

Fatal prion diseases, such as Creutzfeldt-Jakob disease in humans, are associated with the conversion of the normally folded mammalian PrP protein to a misfolded prion form that aggregates. Understanding how prions behave has been greatly facilitated by the study of prions in Saccharomyces cerevisiae, or baker’s yeast. In yeast, the translation release factor, Sup35, misfolds to form the [PSI+] prion. Although the Sup35 protein has a significantly different primary sequence from PrP, its prion form behaves similarly to human prions. The N-terminus of Sup35 is Q/N-rich and responsible for prion formation. Determining the structure of this region has proven difficult since the N-terminus forms aggregates instead of the ordered crystals required for structural studies. However, a small seven amino acid sequence (GNNQQNY) from Sup35's N-terminus was crystallized by Nelson et al. (2005). We have constructed a 3D physical model of GNNQQNY as part of the MSOE SMART Teams program using 3D printing technology. GNNQQNY's structure suggests that multiple prion molecules assemble into strong fibrous aggregates through tightly structured interlocking parallel beta sheets called a cross-β spine. The structure of GNNQQNY suggests a potential model of how human prions assemble, which could potentially help in developing therapies that prevent aggregation. Supported by a grant from NIH-NCRR-SEPA.

{{Clear}}

==Creating the Physical Model of GNNQQNY==

<applet load='1yjp.pdb' size='400' frame='true' align='left' caption='Community SMART Team Model - GNNQQNY from Yeast Prion Sup35' scene='User:David_Stack/Workbench/1yjp_our_version/9'/>

Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. To design our model of the structure of the GNNQQNY from yeast prion Sup35, we used the atomic coordinates for this structure as reported in the pdb file 1yjp, from the Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics.

Beginning with <scene name='User:David_Stack/Workbench/Prion_step_one/1'>the raw 1yjp pdb file</scene>, the format was set to ball and stick and the spacefill set to 225. The <scene name='User:David_Stack/Workbench/Prion_step_two/1'>water molecules were deleted </scene> and half the model was <scene name='User:David_Stack/Workbench/Prion_step_three/1'> colored cyan </scene> to represent the wet interface. The dry interface was <scene name='User:David_Stack/Workbench/Prion_step_three_and_a_half/1'> colored blue </scene> and the backbone was <scene name='User:David_Stack/Workbench/Prion_step_four/1'> colored white. </scene> The <scene name='User:David_Stack/Workbench/Prion_step_five/1'> oxygen molecules </scene> were colored red for Asn2 and Asn3, orange for Gln4 and Gln5 and yellow for Asn6 and Tyr7.

A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer.

{{Clear}}

==References==
1) Nelson, R., Sawaya, MR., Balbirnie, M., Madsen, AO., Riekel, C., Grothe, R. & Eisenberg, D. (2005). Structure of the cross ß-spine of amyloid-like fibrils. Nature. 435, 773-778.

2) Shkundina, I.S. & Ter-Avanesyan, M.D. (2007). Prions. Biochemistry (Moscow). 72:13, 1519-1536.

{{Clear}}

==Our Poster and Presentations==
[[Image:CommunitySMARTTeamwithMentor.jpg|Community SMART Team with Mentor| 350px]]
[[Image:Community_SMART_Team_GNNQQNY.jpg|Community SMART Team Poster| 350px]]

{{Clear}}

Presentations of our project, poster, and physical models:

-- Medical College of Wisconsin SMART Team Poster Session, March 6, 2009

-- American Society for Biochemistry and Molecular Biology Undergraduate Research Poster Competition, April 18, 2009

-- University of Wisconsin Milwaukee Undergraduate Research Symposium, April 24, 2009

{{Clear}}

==MSOE Center for BioMolecular Modeling and SMART Teams==
[[Image:Center for BioMolecular Modeling Logo.jpg|left|200px]]
[[Image:Smart Teams photo 5.jpg|right|120px]]

SMART Teams (Students Modeling A Research Topic) is a science outreach program developed by the MSOE Center for BioMolecular Modeling. In this program, teams of high school students work with a local resarch lab to design and build a physical model of a protein that is being investigated by the lab. The goal of the SMART Team program is to introduce students to the real world of science --- as it exists in a local research lab. The development of this program was supported by grants from the NIH-NCRR SEPA program (Science Education Partnership Award) and an HHMI Precollege Science Education Award. For more information about this program, visit the CBM web site at [http://www.rpc.msoe.edu/cbm www.rpc.msoe.edu/cbm] .

Group:SMART:A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35

2009-04-09T16:19:20Z

David Stack:

=='''A SMART Team Molecular Story --- from the 2009 Community SMART Team of Southeast Wisconsin'''==

:Students -- Moses Misplon, Meghan Murphy, Joel Pollen, Christine Pollnow, Maia Stack

:Advisor: David Stack, Ph.D., University of Wisconsin–Milwaukee

:Mentors: Anita Manogaran, Ph.D., University of Illinois at Chicago
<applet load='1yjp_our_version' size='300' frame='true' align='right' caption='GNNQQNY - a section of the [PSI+] prion' scene='User:David_Stack/Workbench/Movie_companion/3' />

<swf> http://myweb.msoe.edu/~hoelzer/Community%202008-2009.swf</swf>

{{clear}}

==Abstract for Our Project==

Fatal prion diseases, such as Creutzfeldt-Jakob disease in humans, are associated with the conversion of the normally folded mammalian PrP protein to a misfolded prion form that aggregates. Understanding how prions behave has been greatly facilitated by the study of prions in Saccharomyces cerevisiae, or baker’s yeast. In yeast, the translation release factor, Sup35, misfolds to form the [PSI+] prion. Although the Sup35 protein has a significantly different primary sequence from PrP, its prion form behaves similarly to human prions. The N-terminus of Sup35 is Q/N-rich and responsible for prion formation. Determining the structure of this region has proven difficult since the N-terminus forms aggregates instead of the ordered crystals required for structural studies. However, a small seven amino acid sequence (GNNQQNY) from Sup35's N-terminus was crystallized by Nelson et al. (2005). We have constructed a 3D physical model of GNNQQNY as part of the MSOE SMART Teams program using 3D printing technology. GNNQQNY's structure suggests that multiple prion molecules assemble into strong fibrous aggregates through tightly structured interlocking parallel beta sheets called a cross-β spine. The structure of GNNQQNY suggests a potential model of how human prions assemble, which could potentially help in developing therapies that prevent aggregation. Supported by a grant from NIH-NCRR-SEPA.

{{Clear}}

==Creating the Physical Model of GNNQQNY==

<applet load='1yjp.pdb' size='400' frame='true' align='left' caption='Community SMART Team Model - GNNQQNY from Yeast Prion Sup35' scene='User:David_Stack/Workbench/1yjp_our_version/9'/>

Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. To design our model of the structure of the GNNQQNY from yeast prion Sup35, we used the atomic coordinates for this structure as reported in the pdb file 1yjp, from the Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics.

Beginning with <scene name='User:David_Stack/Workbench/Prion_step_one/1'>the raw 1yjp pdb file</scene>, the format was set to ball and stick and the spacefill set to 225. The <scene name='User:David_Stack/Workbench/Prion_step_two/1'>water molecules were deleted </scene> and half the model was <scene name='User:David_Stack/Workbench/Prion_step_three/1'> colored cyan </scene> to represent the wet interface. The dry interface was <scene name='User:David_Stack/Workbench/Prion_step_three_and_a_half/1'> colored blue </scene> and the backbone was <scene name='User:David_Stack/Workbench/Prion_step_four/1'> colored white. </scene> The <scene name='User:David_Stack/Workbench/Prion_step_five/1'> oxygen molecules </scene> were colored red for Asn2 and Asn3, orange for Gln4 and Gln5 and yellow for Asn6 and Tyr7.

A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer.

{{Clear}}

==References==
1) Nelson, R., Sawaya, MR., Balbirnie, M., Madsen, AO., Riekel, C., Grothe, R. & Eisenberg, D. (2005). Structure of the cross ß-spine of amyloid-like fibrils. Nature. 435, 773-778.

2) Shkundina, I.S. & Ter-Avanesyan, M.D. (2007). Prions. Biochemistry (Moscow). 72:13, 1519-1536.

{{Clear}}

==Our Poster and Presentations==
[[Image:CommunitySMARTTeamwithMentor.jpg|Community SMART Team with Mentor| 350px]]
[[Image:Community_SMART_Team_GNNQQNY.jpg|Community SMART Team Poster| 350px]]

{{Clear}}

Presentations of our project, poster, and physical models:

-- Medical College of Wisconsin SMART Team Poster Session, March 6, 2009

-- American Society for Biochemistry and Molecular Biology Undergraduate Research Poster Competition, April 18, 2009

-- University of Wisconsin Milwaukee Undergraduate Research Symposium, April 24, 2009

{{Clear}}

==MSOE Center for BioMolecular Modeling and SMART Teams==
[[Image:Center for BioMolecular Modeling Logo.jpg|left|200px]]
[[Image:Smart Teams photo 5.jpg|right|120px]]

SMART Teams (Students Modeling A Research Topic) is a science outreach program developed by the MSOE Center for BioMolecular Modeling. In this program, teams of high school students work with a local resarch lab to design and build a physical model of a protein that is being investigated by the lab. The goal of the SMART Team program is to introduce students to the real world of science --- as it exists in a local research lab. The development of this program was supported by grants from the NIH-NCRR SEPA program (Science Education Partnership Award) and an HHMI Precollege Science Education Award. For more information about this program, visit the CBM web site at [http://www.rpc.msoe.edu/cbm www.rpc.msoe.edu/cbm] .

Group:SMART:A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35

2009-04-09T16:17:25Z

David Stack: New page: =''' A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35 '''= =='''A SMART Team Molecular Story<font color = 'blac...

=''' A Physical Model of the Structure of GNNQQNY from Yeast Prion Sup35 '''=

=='''A SMART Team Molecular Story --- from the 2009 Community SMART Team of Southeast Wisconsin'''==

:Students -- Moses Misplon, Meghan Murphy, Joel Pollen, Christine Pollnow, Maia Stack

:Advisor: David Stack, Ph.D., University of Wisconsin–Milwaukee

:Mentors: Anita Manogaran, Ph.D., University of Illinois at Chicago
<applet load='1yjp_our_version' size='300' frame='true' align='right' caption='GNNQQNY - a section of the [PSI+] prion' scene='User:David_Stack/Workbench/Movie_companion/3' />

<swf> http://myweb.msoe.edu/~hoelzer/Community%202008-2009.swf</swf>

{{clear}}

==Abstract for Our Project==

Fatal prion diseases, such as Creutzfeldt-Jakob disease in humans, are associated with the conversion of the normally folded mammalian PrP protein to a misfolded prion form that aggregates. Understanding how prions behave has been greatly facilitated by the study of prions in Saccharomyces cerevisiae, or baker’s yeast. In yeast, the translation release factor, Sup35, misfolds to form the [PSI+] prion. Although the Sup35 protein has a significantly different primary sequence from PrP, its prion form behaves similarly to human prions. The N-terminus of Sup35 is Q/N-rich and responsible for prion formation. Determining the structure of this region has proven difficult since the N-terminus forms aggregates instead of the ordered crystals required for structural studies. However, a small seven amino acid sequence (GNNQQNY) from Sup35's N-terminus was crystallized by Nelson et al. (2005). We have constructed a 3D physical model of GNNQQNY as part of the MSOE SMART Teams program using 3D printing technology. GNNQQNY's structure suggests that multiple prion molecules assemble into strong fibrous aggregates through tightly structured interlocking parallel beta sheets called a cross-β spine. The structure of GNNQQNY suggests a potential model of how human prions assemble, which could potentially help in developing therapies that prevent aggregation. Supported by a grant from NIH-NCRR-SEPA.

{{Clear}}

==Creating the Physical Model of GNNQQNY==

<applet load='1yjp.pdb' size='400' frame='true' align='left' caption='Community SMART Team Model - GNNQQNY from Yeast Prion Sup35' scene='User:David_Stack/Workbench/1yjp_our_version/9'/>

Virtually any image of a protein that can be created in the computer environment of RP-RasMol, can be converted into a physical model of the protein using rapid prototyping technology. To design our model of the structure of the GNNQQNY from yeast prion Sup35, we used the atomic coordinates for this structure as reported in the pdb file 1yjp, from the Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics.

Beginning with <scene name='User:David_Stack/Workbench/Prion_step_one/1'>the raw 1yjp pdb file</scene>, the format was set to ball and stick and the spacefill set to 225. The <scene name='User:David_Stack/Workbench/Prion_step_two/1'>water molecules were deleted </scene> and half the model was <scene name='User:David_Stack/Workbench/Prion_step_three/1'> colored cyan </scene> to represent the wet interface. The dry interface was <scene name='User:David_Stack/Workbench/Prion_step_three_and_a_half/1'> colored blue </scene> and the backbone was <scene name='User:David_Stack/Workbench/Prion_step_four/1'> colored white. </scene> The <scene name='User:David_Stack/Workbench/Prion_step_five/1'> oxygen molecules </scene> were colored red for Asn2 and Asn3, orange for Gln4 and Gln5 and yellow for Asn6 and Tyr7.

A ply file describing this final structure was exported from RP-RasMol and sent to the MSOE Center for BioMolecular Modeling, where it was constructed from plaster powder, using a color ZCorp 3D printer.

{{Clear}}

==References==
1) Nelson, R., Sawaya, MR., Balbirnie, M., Madsen, AO., Riekel, C., Grothe, R. & Eisenberg, D. (2005). Structure of the cross ß-spine of amyloid-like fibrils. Nature. 435, 773-778.

2) Shkundina, I.S. & Ter-Avanesyan, M.D. (2007). Prions. Biochemistry (Moscow). 72:13, 1519-1536.

{{Clear}}

==Our Poster and Presentations==
[[Image:CommunitySMARTTeamwithMentor.jpg|Community SMART Team with Mentor| 350px]]
[[Image:Community_SMART_Team_GNNQQNY.jpg|Community SMART Team Poster| 350px]]

{{Clear}}

Presentations of our project, poster, and physical models:

-- Medical College of Wisconsin SMART Team Poster Session, March 6, 2009

-- American Society for Biochemistry and Molecular Biology Undergraduate Research Poster Competition, April 18, 2009

-- University of Wisconsin Milwaukee Undergraduate Research Symposium, April 24, 2009

{{Clear}}

==MSOE Center for BioMolecular Modeling and SMART Teams==
[[Image:Center for BioMolecular Modeling Logo.jpg|left|200px]]
[[Image:Smart Teams photo 5.jpg|right|120px]]

SMART Teams (Students Modeling A Research Topic) is a science outreach program developed by the MSOE Center for BioMolecular Modeling. In this program, teams of high school students work with a local resarch lab to design and build a physical model of a protein that is being investigated by the lab. The goal of the SMART Team program is to introduce students to the real world of science --- as it exists in a local research lab. The development of this program was supported by grants from the NIH-NCRR SEPA program (Science Education Partnership Award) and an HHMI Precollege Science Education Award. For more information about this program, visit the CBM web site at [http://www.rpc.msoe.edu/cbm www.rpc.msoe.edu/cbm] .

User:David Stack

2009-04-05T15:32:18Z

David Stack:

David Stack Ph.D. is the Deputy CIO for Strategic Planning at the University of Wisconsin–Milwaukee (UWM) where he earned his doctorate in Engineering. His responsibilities include planning, policy, governance and research computing, and he is particularly interested in integrated, campuswide planning for academics, facilities and technology. He is the volunteer instructor for the molecular modeling activities of the 2009 high school Community SMART Team of Southeast Wisconsin. He also works with educational and cultural non-profit organizations.
*[[User:David Stack/Workbench]]

User:David Stack

2009-04-05T15:31:29Z

David Stack:

David Stack Ph.D. is the Deputy CIO for Strategic Planning at the University of Wisconsin–Milwaukee (UWM) where he earned his doctorate in Engineering. His responsibilities include planning, policy, governance and research computing, and he is particularly interested in integrated, campuswide planning for academics, facilities and technology. He is the volunteer instructor for the molecular modeling activities of the high school Community SMART Team of Southeast Wisconsin. He also works with educational and cultural non-profit organizations.
*[[User:David Stack/Workbench]]

File:CommunitySMARTTeamwithMentor.jpg

2009-04-05T13:31:22Z

David Stack: Mentor Anita Manogaran Ph.D., explains prion aggregation to the 2009 Community SMART Team.

== Summary ==
Mentor Anita Manogaran Ph.D., explains prion aggregation to the 2009 Community SMART Team.
== Licensing ==
{{GFDL}}

File:Community SMART Team GNNQQNY.jpg

2009-04-05T13:21:39Z

David Stack: This is the poster of the GNNQQNY sequence from yeast prion [PSI+] created by the 2009 Community SMART Team of Southeast Wisconsin under the guidance of the Milwaukee School of Engineering Center for BioMolecular Modeling.

== Summary ==
This is the poster of the GNNQQNY sequence from yeast prion [PSI+] created by the 2009 Community SMART Team of Southeast Wisconsin under the guidance of the Milwaukee School of Engineering Center for BioMolecular Modeling.
== Licensing ==
{{GFDL}}