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You searched for +publisher:"The Ohio State University" +contributor:("Magliery, Thomas"). Showing records 1 – 17 of 17 total matches.

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The Ohio State University

1. Li, Weiyi. Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches.

Degree: MS, Chemistry, 2014, The Ohio State University

 The sequence-structure-stability relationship is a key problem in the field of protein science. Although a large amount of research has been working on it in… (more)

Subjects/Keywords: Biochemistry; Chemistry; Biophysics; Biology; Rop, Rosetta, protein G, combinatorial library, hydrophobic core library, computational design, high-throughput

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APA (6th Edition):

Li, W. (2014). Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1398956266

Chicago Manual of Style (16th Edition):

Li, Weiyi. “Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches.” 2014. Masters Thesis, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1398956266.

MLA Handbook (7th Edition):

Li, Weiyi. “Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches.” 2014. Web. 15 Aug 2020.

Vancouver:

Li W. Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches. [Internet] [Masters thesis]. The Ohio State University; 2014. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1398956266.

Council of Science Editors:

Li W. Protein Engineering Hydrophobic Core Residues of Computationally Designed Protein G and Single-Chain Rop: Investigating the Relationship between Protein Primary structure and Protein Stability through High-Throughput Approaches. [Masters Thesis]. The Ohio State University; 2014. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1398956266


The Ohio State University

2. Sen, Shiladitya. Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods.

Degree: PhD, Chemistry, 2013, The Ohio State University

 The inability to accurately decipher the relationship between a protein’s sequence and its structural stability presents a major difficulty in predicting the effects of mutation… (more)

Subjects/Keywords: Chemistry; Biochemistry; Protein engineering, High-throughput, Stability, Combinatorial library,Antibodies

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APA (6th Edition):

Sen, S. (2013). Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1385987653

Chicago Manual of Style (16th Edition):

Sen, Shiladitya. “Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods.” 2013. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1385987653.

MLA Handbook (7th Edition):

Sen, Shiladitya. “Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods.” 2013. Web. 15 Aug 2020.

Vancouver:

Sen S. Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods. [Internet] [Doctoral dissertation]. The Ohio State University; 2013. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1385987653.

Council of Science Editors:

Sen S. Engineering Proteins for Enhanced Stability using High-throughput and Combinatorial methods. [Doctoral Dissertation]. The Ohio State University; 2013. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1385987653


The Ohio State University

3. Harsch, Christina I K. Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1.

Degree: PhD, Chemistry, 2011, The Ohio State University

 There are limited efficient methods in treating organophosphorus (OP)-poisoning through exposure to pesticides and nerve agents. Human paraoxonase-1 (PON1) is a calcium-dependent enzyme that is… (more)

Subjects/Keywords: Biochemistry; Chemistry; paraoxonase-1; PON1

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APA (6th Edition):

Harsch, C. I. K. (2011). Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1325197473

Chicago Manual of Style (16th Edition):

Harsch, Christina I K. “Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1.” 2011. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1325197473.

MLA Handbook (7th Edition):

Harsch, Christina I K. “Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1.” 2011. Web. 15 Aug 2020.

Vancouver:

Harsch CIK. Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1. [Internet] [Doctoral dissertation]. The Ohio State University; 2011. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1325197473.

Council of Science Editors:

Harsch CIK. Mutagenic Studies of Substrate Specificity and Stability of Paraoxonase-1. [Doctoral Dissertation]. The Ohio State University; 2011. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1325197473


The Ohio State University

4. Sarkar, Mohosin M. Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility.

Degree: PhD, Chemistry, 2009, The Ohio State University

  Protein–protein interactions (PPIs) play a key role in most biological processes. Many of these interactions are necessary for cell survival. To understand the molecular… (more)

Subjects/Keywords: Biochemistry; Chemistry; Molecular Biology; Protein-protein interactions; Split GFP assay; Split GFP reassembly; BRCA1/BARD1 interactions; BRCA1 cancer associated mutations; Human paraoxonase-1

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APA (6th Edition):

Sarkar, M. M. (2009). Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776

Chicago Manual of Style (16th Edition):

Sarkar, Mohosin M. “Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility.” 2009. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.

MLA Handbook (7th Edition):

Sarkar, Mohosin M. “Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility.” 2009. Web. 15 Aug 2020.

Vancouver:

Sarkar MM. Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility. [Internet] [Doctoral dissertation]. The Ohio State University; 2009. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.

Council of Science Editors:

Sarkar MM. Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility. [Doctoral Dissertation]. The Ohio State University; 2009. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776


The Ohio State University

5. Nguyen, Chau Q. Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches.

Degree: MS, Chemistry, 2010, The Ohio State University

 Recent developments in the field of rational engineering have increased the awareness that surface residues and surface electrostatics of proteins are more important for protein… (more)

Subjects/Keywords: Chemistry

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APA (6th Edition):

Nguyen, C. Q. (2010). Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1281719548

Chicago Manual of Style (16th Edition):

Nguyen, Chau Q. “Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches.” 2010. Masters Thesis, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1281719548.

MLA Handbook (7th Edition):

Nguyen, Chau Q. “Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches.” 2010. Web. 15 Aug 2020.

Vancouver:

Nguyen CQ. Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches. [Internet] [Masters thesis]. The Ohio State University; 2010. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1281719548.

Council of Science Editors:

Nguyen CQ. Protein Engineering Surface Residues of the Four-helix Bundle Protein Rop: Evaluating the Relationship of Sequence-Stability through High-Throughput Approaches. [Masters Thesis]. The Ohio State University; 2010. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1281719548


The Ohio State University

6. Lavinder, Jason James. Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering.

Degree: PhD, Ohio State Biochemistry Program, 2009, The Ohio State University

  The inability to accurately decipher the relationship between protein sequence and structural stability presents a major difficulty in predicting the effects of mutation on… (more)

Subjects/Keywords: Biochemistry; protein engineering; protein biophysics; protein stability

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APA (6th Edition):

Lavinder, J. J. (2009). Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1245427976

Chicago Manual of Style (16th Edition):

Lavinder, Jason James. “Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering.” 2009. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1245427976.

MLA Handbook (7th Edition):

Lavinder, Jason James. “Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering.” 2009. Web. 15 Aug 2020.

Vancouver:

Lavinder JJ. Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering. [Internet] [Doctoral dissertation]. The Ohio State University; 2009. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1245427976.

Council of Science Editors:

Lavinder JJ. Analyzing the Sequence-Stability Landscape of the Four-helix Bundle Protein Rop: Developing High-Throughput Approaches for Combinatorial Biophysics and Protein Engineering. [Doctoral Dissertation]. The Ohio State University; 2009. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1245427976


The Ohio State University

7. Sullivan, Brandon Joseph. Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase.

Degree: PhD, Biochemistry Program, Ohio State, 2011, The Ohio State University

  The structure, function and dynamics of proteins are determined by the physical and chemical properties of their amino acids. Unfortunately, the information encapsulated within… (more)

Subjects/Keywords: Biochemistry; Bioinformatics; Biophysics; Molecular Biology; Protein Engineering; Protein Sequence Statistics; Triosephosphate Isomerase

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APA (6th Edition):

Sullivan, B. J. (2011). Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1325106135

Chicago Manual of Style (16th Edition):

Sullivan, Brandon Joseph. “Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase.” 2011. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1325106135.

MLA Handbook (7th Edition):

Sullivan, Brandon Joseph. “Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase.” 2011. Web. 15 Aug 2020.

Vancouver:

Sullivan BJ. Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase. [Internet] [Doctoral dissertation]. The Ohio State University; 2011. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1325106135.

Council of Science Editors:

Sullivan BJ. Engineering Proteins from Sequence Statistics: Identifying and Understanding the Roles of Conservation and Correlation in Triosephosphate Isomerase. [Doctoral Dissertation]. The Ohio State University; 2011. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1325106135


The Ohio State University

8. Durani, Venuka. The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain.

Degree: PhD, Chemistry, 2012, The Ohio State University

  The protein folding problem is an ongoing challenge, and even though there have been significant advances in our understanding of proteins, accurately predicting the… (more)

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APA (6th Edition):

Durani, V. (2012). The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1338311626

Chicago Manual of Style (16th Edition):

Durani, Venuka. “The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain.” 2012. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1338311626.

MLA Handbook (7th Edition):

Durani, Venuka. “The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain.” 2012. Web. 15 Aug 2020.

Vancouver:

Durani V. The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain. [Internet] [Doctoral dissertation]. The Ohio State University; 2012. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1338311626.

Council of Science Editors:

Durani V. The Cycle of Protein Engineering: Bioinformatics Design of Two Dimeric Proteins and Computational Design of a Small Globular Domain. [Doctoral Dissertation]. The Ohio State University; 2012. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1338311626


The Ohio State University

9. Mata, David Garcia. Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids.

Degree: PhD, Chemistry, 2012, The Ohio State University

 Rational design is a powerful tool that can be used to understand the function of a protein, enhance a desired function, or engineer novel functionalities… (more)

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APA (6th Edition):

Mata, D. G. (2012). Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1338392020

Chicago Manual of Style (16th Edition):

Mata, David Garcia. “Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids.” 2012. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1338392020.

MLA Handbook (7th Edition):

Mata, David Garcia. “Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids.” 2012. Web. 15 Aug 2020.

Vancouver:

Mata DG. Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids. [Internet] [Doctoral dissertation]. The Ohio State University; 2012. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1338392020.

Council of Science Editors:

Mata DG. Understanding Protein Structure And Function Using Rational Design And Unnatural Amino Acids. [Doctoral Dissertation]. The Ohio State University; 2012. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1338392020


The Ohio State University

10. Mohan, Sidharth. Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability.

Degree: PhD, Biophysics, 2017, The Ohio State University

 Proteins represent the most diverse class of molecules that form the biochemical basis of life, and are products of the innumerable ways in which the… (more)

Subjects/Keywords: Biophysics; protein engineering, statistical sequence design, consensus, correlations, triosephosphate isomerase, stability

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APA (6th Edition):

Mohan, S. (2017). Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1503054678218166

Chicago Manual of Style (16th Edition):

Mohan, Sidharth. “Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability.” 2017. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1503054678218166.

MLA Handbook (7th Edition):

Mohan, Sidharth. “Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability.” 2017. Web. 15 Aug 2020.

Vancouver:

Mohan S. Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability. [Internet] [Doctoral dissertation]. The Ohio State University; 2017. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1503054678218166.

Council of Science Editors:

Mohan S. Consensus, Correlation And Combinatorics Based Approaches In Engineering And Exploring Triosephosphate Isomerase Stability. [Doctoral Dissertation]. The Ohio State University; 2017. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1503054678218166


The Ohio State University

11. Callahan, Nicholas. Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase.

Degree: PhD, Biophysics, 2015, The Ohio State University

 Despite the large databases of protein sequence and structure data presently available, predicting the effect of mutations on an enzyme is still a major challenge.… (more)

Subjects/Keywords: Biophysics; Protein engineering; correlation; co-mutation; consensus proteins; Adenylate kinase

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APA (6th Edition):

Callahan, N. (2015). Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1420802270

Chicago Manual of Style (16th Edition):

Callahan, Nicholas. “Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase.” 2015. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1420802270.

MLA Handbook (7th Edition):

Callahan, Nicholas. “Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase.” 2015. Web. 15 Aug 2020.

Vancouver:

Callahan N. Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase. [Internet] [Doctoral dissertation]. The Ohio State University; 2015. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1420802270.

Council of Science Editors:

Callahan N. Bioinformatics-Driven Enzyme Engineering: Work On Adenylate Kinase. [Doctoral Dissertation]. The Ohio State University; 2015. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1420802270


The Ohio State University

12. Visco, Michael David. Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization.

Degree: PhD, Chemistry, 2017, The Ohio State University

 Molecular recognition by hydrogen-bond donors has proven to be applicable to various areas of research, including sensing and catalysis. (Thio)ureas have been established as the… (more)

Subjects/Keywords: Chemistry; Organic Chemistry; silanediols; benzylic silanes; organocatalysis; anion-binding catalysis; chromanone

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APA (6th Edition):

Visco, M. D. (2017). Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1492438099945523

Chicago Manual of Style (16th Edition):

Visco, Michael David. “Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization.” 2017. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1492438099945523.

MLA Handbook (7th Edition):

Visco, Michael David. “Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization.” 2017. Web. 15 Aug 2020.

Vancouver:

Visco MD. Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization. [Internet] [Doctoral dissertation]. The Ohio State University; 2017. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1492438099945523.

Council of Science Editors:

Visco MD. Chiral Silanediols Designed for Enantioselective Heterocycle Functionalization. [Doctoral Dissertation]. The Ohio State University; 2017. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1492438099945523


The Ohio State University

13. Baldauff, Rachel Michelle. Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins.

Degree: MS, Chemistry, 2011, The Ohio State University

 Overwhelming evidence suggests that low levels of high-density lipoproteins (HDL) increase one’s odds of developing coronary artery disease (CAD). This phenomenon could be due in… (more)

Subjects/Keywords: Biochemistry; rePON1; rHDL; G3C9

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APA (6th Edition):

Baldauff, R. M. (2011). Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1321986125

Chicago Manual of Style (16th Edition):

Baldauff, Rachel Michelle. “Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins.” 2011. Masters Thesis, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1321986125.

MLA Handbook (7th Edition):

Baldauff, Rachel Michelle. “Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins.” 2011. Web. 15 Aug 2020.

Vancouver:

Baldauff RM. Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins. [Internet] [Masters thesis]. The Ohio State University; 2011. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1321986125.

Council of Science Editors:

Baldauff RM. Interaction of Recombinant Paraoxonase-1 with Reconstituted High-Density Lipoproteins. [Masters Thesis]. The Ohio State University; 2011. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1321986125

14. Panneerselvam, Nishanthi. Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing.

Degree: MS, Biophysics, 2013, The Ohio State University

 High throughput DNA sequencing technologies have revolutionized the field ofgenomics. It is now possible to generate huge amounts of sequencing data at significantlylower costs and… (more)

Subjects/Keywords: Biophysics; Biochemistry; Deep sequencing; Illumina sequencing; ROP

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APA (6th Edition):

Panneerselvam, N. (2013). Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1376954254

Chicago Manual of Style (16th Edition):

Panneerselvam, Nishanthi. “Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing.” 2013. Masters Thesis, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1376954254.

MLA Handbook (7th Edition):

Panneerselvam, Nishanthi. “Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing.” 2013. Web. 15 Aug 2020.

Vancouver:

Panneerselvam N. Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing. [Internet] [Masters thesis]. The Ohio State University; 2013. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1376954254.

Council of Science Editors:

Panneerselvam N. Exploring the Sequence Landscape of the Four-helix Bundle Protein ROP using DeepSequencing. [Masters Thesis]. The Ohio State University; 2013. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1376954254

15. Panneerselvam, Nishanthi. Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins.

Degree: PhD, Biophysics, 2017, The Ohio State University

 Surface residues and surface electrostatics play an active role in maintaining protein stability. A combinatorial library randomizing five surface positions in Rop to NNK (K=G… (more)

Subjects/Keywords: Biochemistry; Biophysics; Molecular Biology

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APA (6th Edition):

Panneerselvam, N. (2017). Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1492735031524266

Chicago Manual of Style (16th Edition):

Panneerselvam, Nishanthi. “Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins.” 2017. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1492735031524266.

MLA Handbook (7th Edition):

Panneerselvam, Nishanthi. “Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins.” 2017. Web. 15 Aug 2020.

Vancouver:

Panneerselvam N. Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins. [Internet] [Doctoral dissertation]. The Ohio State University; 2017. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1492735031524266.

Council of Science Editors:

Panneerselvam N. Exploring the sequence landscape of the model protein Rop to gain insights into sequence-stability relationship in proteins. [Doctoral Dissertation]. The Ohio State University; 2017. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1492735031524266

16. Kumar, Anusha. Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches.

Degree: PhD, Chemistry, 2019, The Ohio State University

 A fundamental challenge of protein engineering is the ability to consistently design proteins that will spontaneously fold into `native-like’ structures. Combinatorial de novo design offers… (more)

Subjects/Keywords: Chemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Kumar, A. (2019). Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches. (Doctoral Dissertation). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1546476128094184

Chicago Manual of Style (16th Edition):

Kumar, Anusha. “Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches.” 2019. Doctoral Dissertation, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1546476128094184.

MLA Handbook (7th Edition):

Kumar, Anusha. “Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches.” 2019. Web. 15 Aug 2020.

Vancouver:

Kumar A. Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches. [Internet] [Doctoral dissertation]. The Ohio State University; 2019. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1546476128094184.

Council of Science Editors:

Kumar A. Exploring packing defects, loop interactions and sequence-fitness landscape in a four-helix bundle protein Rop, by combinatorial and high-throughput approaches. [Doctoral Dissertation]. The Ohio State University; 2019. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1546476128094184

17. Craigo, Kevin Alan. Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin.

Degree: MS, Chemistry, 2011, The Ohio State University

  It is well known that proteins play essential roles in the proper functioning of all biological systems. Protein hydration dynamics are of fundamental importance… (more)

Subjects/Keywords: Biochemistry; Biology; Chemistry; Physical Chemistry; Physics; hydration; calmodulin; conformation; spectroscopic; ultrafast; femtosecond; up-conversion; solvation; tryptophan; protein

…Teaching Associate, Department of Chemistry, The Ohio State University FIELDS OF STUDY Major… 

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Craigo, K. A. (2011). Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1311089745

Chicago Manual of Style (16th Edition):

Craigo, Kevin Alan. “Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin.” 2011. Masters Thesis, The Ohio State University. Accessed August 15, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1311089745.

MLA Handbook (7th Edition):

Craigo, Kevin Alan. “Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin.” 2011. Web. 15 Aug 2020.

Vancouver:

Craigo KA. Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin. [Internet] [Masters thesis]. The Ohio State University; 2011. [cited 2020 Aug 15]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1311089745.

Council of Science Editors:

Craigo KA. Ultrafast Spectroscopic Study of Hydration and Conformational Dynamics in Calmodulin. [Masters Thesis]. The Ohio State University; 2011. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1311089745

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