|
|
| Home | Database | Software | Help | Research | Authoring |
|
Home >> Database >> Activities >> View |
In the Database section: Introduction | Search | Browse |
|
Protein Conservation: an View into Proteomics
This Activity Requires:
Test your system to see if it meets the requirements Important! If you cannot launch anything from this database, please follow the step-by-step instructions on the software page. Please Note: Many models are linked to directly from within the database. When an activity employs our scripting language, Pedagogica, as do some of the "guided" activities, the initial download may take several minutes. Subsequent activities will not take a long time. See this page for further instructions. |
||||||||||||||
![]() | Overview and Learning ObjectivesStudents review aspects of protein structure and folding and then move to 3D molecules, evaluating the consequences of both conservative and non-conservative substitutions in protein sequences. The activity culminates in a comparison of human, rat and bacterial enzymes; students discuss why it is be important for some regions to be conserved. Students will be able to: • explain the basic forces at work in protein folding • differentiate conservative and non-conservative substitutions in mutations. • compare human, rat and bacterial enzymes and discuss why it is be important for some to be conserved. |
|
| |
|
| |
|
| |
![]() | Central ConceptsKey Concept: Finding similarities in sequences is greatly aided by computers. Additional Related ConceptsMolecular Biology
|
|
| |
|
| |
|
| |
![]() | Textbook References
|
|
| |
|
| |
|
| |
![]() | Activity CreditsCreated by CC: Molecular Literacy using Molecular Workbench |
|
| |
|
| |
|
| |
![]() | Requirements
|
|
| |
|
| |
|
| |
Last Update: 11/25/2008
Maintainer: CC Web Team (webmaster@concord.org)
Document Options: Text-only / Accessible Version | Printable Version | E-mail this Page
Copyright © 2008, The Concord Consortium.
All rights reserved.
![]()
These materials are based upon work supported
by the National Science Foundation under grant numbers
9980620, ESI-0242701 and EIA-0219345
Any opinions, findings, and conclusions or recommendations expressed in this
material are those of the author(s) and do not necessarily reflect
the views of the National Science Foundation.