User:Alexander Cvitan/Notebook/Experimental Biological Chemistry Lab/2014/02/05: Difference between revisions
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* A bulk amount of pepsin was added to a single tube of 50:1 AuNP's. We only made one tube of this because in theory the pepsin should chew up the protein on the AuNP's and make the protein loose its function. We just thought if anything should be able to break apart these fibers if the stability is due to the protein it would be pepsin. | * A bulk amount of pepsin was added to a single tube of 50:1 AuNP's. We only made one tube of this because in theory the pepsin should chew up the protein on the AuNP's and make the protein loose its function. We just thought if anything should be able to break apart these fibers if the stability is due to the protein it would be pepsin. | ||
===Data=== | |||
*Looking at the chelator tubes and the pH effected tubes it didn't appear that any treatments were able to break apart the fibers. | |||
*One interesting result was 2,2 bipyridine was apart to make fibers fall out of solution in a 40:1 ratio tube unlike any other treatment. | |||
In addition, it appears that more acidic solutions also made AuNP's fall out of solution in the 40:1 ratio tubes. Basic pH seemed to allow the AuNP's to say suspended but could reverse the process of fiber formation. | |||
*It didn't appears that their was a clear difference between associating and non-associating bases when looking at pH. | |||
*These are just sketch of what we saw. Next class we will be taking pictures of each treatment for a more detailed level of analysis. | |||
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Revision as of 19:04, 8 February 2014
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Purpose/Objective
Pre-Procedure Data
ProcedureSolvent Tests
Ionic Strength
Random Tests
Data
In addition, it appears that more acidic solutions also made AuNP's fall out of solution in the 40:1 ratio tubes. Basic pH seemed to allow the AuNP's to say suspended but could reverse the process of fiber formation.
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