Sandbox2O14: Difference between revisions

(One intermediate revision by the same user not shown)

Line 8:

== Overview ==

Through the 2024-2025 Spring Semester at Elizabethtown College, analysis of protein 2O14 was performed to determine its enzymatic function and protein class. Determining the function of unknown proteins is beneficial to help understand biological processes. For 2O14 in particular, this protein was found in ''Bacillus subtilis'' from soil and the gastoinestrial tract of ruminants and humans. Understanding its enzymatic function will pinpoint exactly how this organism interacts with the environment and humans.

2O14 exists as monomeric protein complex. Using SPRITE and Chimera revealed one chain that is very long and does not replicate the amino acid chain. This was further confirmed by looking at the X-ray structure of protein 2O14 and it is stating that there is only one unique protein chain. The chain is 366 residues long and the entire complex has a molecular weight of approximately 41.79kDa.

Line 47:

Line 49:

== Protein Extraction ==

The protein was grown inside of ''E.coli'' with a His-tag for resistance to the antibiotic, Ampicillin. Once the protein was grown, the protein solution was centrifuged and sonicated multiple times to extract the expressed protein. For purification, the protein solution was ran through a Ni-NTA column gathering approximately 3 mL of protein elutions in total.

The protein was grown inside of ''E.coli'' with a His-tag for resistance to the antibiotic, Ampicillin. Once the protein was grown, the protein solution was centrifuged and sonicated multiple times to extract the expressed protein. For purification, the protein solution was ran through a Ni-NTA column gathering approximately 5 mL of protein elutions in total.

== Figure 4 ==

Sandbox2O14: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 8: / Line 8: @@
 == Overview ==
+Through the 2024-2025 Spring Semester at Elizabethtown College, analysis of protein 2O14 was performed to determine its enzymatic function and protein class. Determining the function of unknown proteins is beneficial to help understand biological processes. For 2O14 in particular, this protein was found in ''Bacillus subtilis'' from soil and the gastoinestrial tract of ruminants and humans. Understanding its enzymatic function will pinpoint exactly how this organism interacts with the environment and humans.
 O14 exists as monomeric protein complex. Using SPRITE and Chimera revealed one chain that is very long and does not replicate the amino acid chain. This was further confirmed by looking at the X-ray structure of protein 2O14 and it is stating that there is only one unique protein chain. The chain is 366 residues long and the entire complex has a molecular weight of approximately 41.79kDa.
@@ Line 47: / Line 49: @@
 == Protein Extraction ==
-The protein was grown inside of ''E.coli'' with a His-tag for resistance to the antibiotic, Ampicillin. Once the protein was grown, the protein solution was centrifuged and sonicated multiple times to extract the expressed protein. For purification, the protein solution was ran through a Ni-NTA column gathering approximately 3 mL of protein elutions in total.
+The protein was grown inside of ''E.coli'' with a His-tag for resistance to the antibiotic, Ampicillin. Once the protein was grown, the protein solution was centrifuged and sonicated multiple times to extract the expressed protein. For purification, the protein solution was ran through a Ni-NTA column gathering approximately 5 mL of protein elutions in total.
 == Figure 4 ==