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'''Circular Dichromism and NMR'''

In order to find more about the transciptional and biological activity of c-myc more about it's structure and heterodimerization had to be known. The two main techinques used to identify the bHLH-LZ domains of c-myc were [http://en.wikipedia.org/wiki/Circular_dichroism Circular Dichromism] and [http://en.wikipedia.org/wiki/NMR Nuclear Magnetic Resonance(NMR)]. The CD spectrum was used to compare v-myc with c-myc to identify alpha helical characteristics of the protein. It was also revealed through the CD that the c-myc/max heterodimer is more stable than the max/mad heterodimer. [http://en.wikipedia.org/wiki/Electrophoretic_mobility_shift_assay Electrophoretic Mobility shift assays(EMSA] were use to determine c-myc's function in binding DNA. NMR was used to determine the hydrophobic core formed upon formation of the heterodimeric Myc-Max protein complex the functions in binding DNA<ref>PMID:11292350</ref>.

In order to find more about the transciptional and biological activity of c-myc more about it's structure and heterodimerization had to be known. The two main techinques used to identify the bHLH-LZ domains of c-myc were [http://en.wikipedia.org/wiki/Circular_dichroism Circular Dichromism(CD)] and [http://en.wikipedia.org/wiki/NMR Nuclear Magnetic Resonance(NMR)]. The CD spectrum was used to compare v-myc with c-myc to identify alpha helical characteristics of the protein. It was also revealed through the CD that the c-myc/max heterodimer is more stable than the max/mad heterodimer. [http://en.wikipedia.org/wiki/Electrophoretic_mobility_shift_assay Electrophoretic Mobility shift assays(EMSA)] were use to determine c-myc's function in binding DNA. NMR was used to determine the hydrophobic core formed upon formation of the heterodimeric Myc-Max protein complex the functions in binding DNA<ref>PMID:11292350</ref>.

== Mechanism ==

Sandbox Reserved 452: Difference between revisions

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@@ Line 19: / Line 19: @@
 '''Circular Dichromism and NMR'''
-In order to find more about the transciptional and biological activity of c-myc more about it's structure and heterodimerization had to be known. The two main techinques used to identify the bHLH-LZ domains of c-myc were [http://en.wikipedia.org/wiki/Circular_dichroism Circular Dichromism] and [http://en.wikipedia.org/wiki/NMR Nuclear Magnetic Resonance(NMR)]. The CD spectrum was used to compare v-myc with c-myc to identify alpha helical characteristics of the protein. It was also revealed through the CD that the c-myc/max heterodimer is  more stable than the max/mad heterodimer. [http://en.wikipedia.org/wiki/Electrophoretic_mobility_shift_assay Electrophoretic Mobility shift assays(EMSA] were use to determine c-myc's function in binding DNA. NMR was used to determine the hydrophobic core formed upon formation of the heterodimeric Myc-Max protein complex the functions in binding DNA<ref>PMID:11292350</ref>.
+In order to find more about the transciptional and biological activity of c-myc more about it's structure and heterodimerization had to be known. The two main techinques used to identify the bHLH-LZ domains of c-myc were [http://en.wikipedia.org/wiki/Circular_dichroism Circular Dichromism(CD)] and [http://en.wikipedia.org/wiki/NMR Nuclear Magnetic Resonance(NMR)]. The CD spectrum was used to compare v-myc with c-myc to identify alpha helical characteristics of the protein. It was also revealed through the CD that the c-myc/max heterodimer is  more stable than the max/mad heterodimer. [http://en.wikipedia.org/wiki/Electrophoretic_mobility_shift_assay Electrophoretic Mobility shift assays(EMSA)] were use to determine c-myc's function in binding DNA. NMR was used to determine the hydrophobic core formed upon formation of the heterodimeric Myc-Max protein complex the functions in binding DNA<ref>PMID:11292350</ref>.
 == Mechanism ==