Jasmine Davila Chem430 F16 - Revision history

Jda: /* Proposal */

2016-09-29T02:51:47Z

Proposal

Jda: /* Instruments to be used */

2016-09-29T02:40:54Z

Instruments to be used

Jda: /* Research Times */

2016-09-29T02:38:46Z

Research Times

Jda: /* References (2 minimum) */

2016-09-29T02:38:25Z

References (2 minimum)

Jda: /* Proposal */

2016-09-29T02:38:02Z

Proposal

Jda: /* Proposed Research Project */

2016-09-29T02:36:28Z

Proposed Research Project

Jda: Created page with "SChemistry/Biochemistry Research 430 :Fall 2016 :Jasmine Davila :Senior Biochemistry Major ==Research Times== Tuesday 8-12 : section 01 ==Proposed Research Project== ===En..."

2016-08-26T21:18:37Z

Created page with "SChemistry/Biochemistry Research 430 :Fall 2016 :Jasmine Davila :Senior Biochemistry Major ==Research Times== Tuesday 8-12 : section 01 ==Proposed Research Project== ===En..."

New page

SChemistry/Biochemistry Research 430
:Fall 2016
:Jasmine Davila
:Senior Biochemistry Major

==Research Times==
Tuesday 8-12
: section 01

==Proposed Research Project==
===Enter Project Title here===

===General Information===
:Advisor: Laura Moore
:Other research student collaborators: here
:Other Research Collaborators: here

===Proposal===

===Instruments to be used===

===References (2 minimum)===

===Research pledge===
I, Jasmine Davila, have read the Chem/Bioc 430 course syllabus and understand the general structure and expectations of the research program. The above material was prepared after consultation, and in conjunction with my research advisor.

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 ===Proposal===
-Iron sulfur cluster regulator (IscR) is an Fe-S protein that functions as a transcriptional regulator of Fe-S production and other Fe-S protein encoding genes in Escherichia coli (E. coli.). IscR controls the expression of more than 40 genes in E. coli (1). The purification of IscR for studying its many properties in E. coli has been done many times before.
+Iron sulfur cluster regulator (IscR) is an Fe-S protein that functions as a transcriptional regulator of Fe-S production and other Fe-S protein encoding genes in Escherichia coli (E. coli.). IscR controls the expression of more than 40 genes in E. coli (1). The purification of IscR for studying its many properties in E. coli is a well known technique.
-Recently, Atomic Force Microscopy (AFM) has provided a means of studying receptor ligand interactions that were once not available to us. The NTA-His6 system has shown promise of being an efficient and powerful platform for the stable oriented immobilization of proteins in AFM single-molecule studies (2). We plan to use His-tag sequencing to bind our IscR protein and DNA to a nickel platform and investigate the binding strength of IscR to DNA using AFM techniques.
+Recently, Atomic Force Microscopy (AFM) has provided a means of studying receptor ligand interactions that were once not available to us. Using the NTA-His6 system as a platform for the isolated protein and DNA has shown promise of being an efficient way to study desired single-molecule interactions in a stable manner with AFM (2). We thus plan to use His-tag sequencing to bind our IscR protein and DNA to a nickel platform and investigate the binding strength of IscR to DNA using AFM techniques.
 ===Instruments to be used===

@@ Line 21: / Line 21: @@
 ===Instruments to be used===
 AFM (atomic force microscope)
 Sonicator
 Ultra Centrifuge
 Nickel Column
 SDS PAGE
 ===References (2 minimum)===

@@ Line 18: / Line 18: @@
 ===Proposal===
 Iron sulfur cluster regulator (IscR) is an Fe-S protein that functions as a transcriptional regulator of Fe-S production and other Fe-S protein encoding genes in Escherichia coli (E. coli.). IscR controls the expression of more than 40 genes in E. coli (1). The purification of IscR for studying its many properties in E. coli has been done many times before.
-Recently, Atomic Force Microscopy Microscope (AFM) has provided a means of studying receptor ligand interactions that were once not available to us. The NTA-His6 system has shown promise of being an efficient and powerful platform for the stable oriented immobilization of proteins in AFM single-molecule studies (2). We plan to use His-tag sequencing to bind our IscR protein and DNA to a nickel platform and investigate the binding strength of IscR to DNA using AFM techniques.
+Recently, Atomic Force Microscopy (AFM) has provided a means of studying receptor ligand interactions that were once not available to us. The NTA-His6 system has shown promise of being an efficient and powerful platform for the stable oriented immobilization of proteins in AFM single-molecule studies (2). We plan to use His-tag sequencing to bind our IscR protein and DNA to a nickel platform and investigate the binding strength of IscR to DNA using AFM techniques.
 ===Instruments to be used===

@@ Line 6: / Line 6: @@
 ==Research Times==
 Tuesday 8-12
 ==Proposed Research Project==

@@ Line 30: / Line 30: @@
 ===References (2 minimum)===
 Schwartz CJ, Giel JL, Patschkowski T, Luther C, Ruzicka FJ, Beinert H, Kiley PJ. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc Natl Acad Sci USA 2001; 98:14895-900 [PubMed: 11742080]
 Verbelen, C., Gruber, H. J., & Dufrêne, Y. F. (2007). The NTA-His6 bond is strong enough for AFM single-molecular recognition studies.Journal of Molecular Recognition: JMR, 20(6), 490–494. doi:10.1002/jmr.833
 ===Research pledge===
 I, Jasmine Davila, have read the Chem/Bioc 430 course syllabus and understand the general structure and expectations of the research program. The above material was prepared after consultation, and in conjunction with my research advisor.

@@ Line 9: / Line 9: @@
 ==Proposed Research Project==
-===Enter Project Title here===
+===IscR Purification from ''Escherichia coli.'' for AFM Study===
 ===General Information===
 :Advisor: Laura Moore
-:Other research student collaborators: here
+:Other research student collaborators: none
-:Other Research Collaborators: here
+:Other Research Collaborators: none
 ===Proposal===
 ===Instruments to be used===
 ===References (2 minimum)===
 ===Research pledge===
 I, Jasmine Davila, have read the Chem/Bioc 430 course syllabus and understand the general structure and expectations of the research program. The above material was prepared after consultation, and in conjunction with my research advisor.