Jacquelyn S. Fetrow

Last updated
Jacquelyn S. Fetrow
15th President, Albright College
In office
2017–2024
Alma mater Albright College (BS)
Pennsylvania State University (PhD)
Profession
  • Computational biophysicist
  • Academic administrator
Known forComputational biophysics

Jacquelyn S. (Jacque) Fetrow (born 1960) is a computational biologist and college administrator who served as the 15th president of Albright College. [1] Before serving as president she served as Provost, Vice President of Academic Affairs, and Professor of Chemistry at the University of Richmond in Richmond, Virginia. [2] Prior to that appointment, she served as Dean of the College at Wake Forest University in Winston-Salem, North Carolina. [3] She also co-founded GeneFormatics, Inc., for which she served as Director and Chief Scientific Officer for four years.

Contents

Early life and education

Fetrow is a native of Camp Hill, Pennsylvania. [4] Her mother, Mildred F. Fetrow, was a public school teacher in the West Shore School District, teaching kindergarten, first grade and second grade for many years. [5] Her father, David E. Fetrow, was a carpenter. He also worked as a truck salesman, real estate salesman, and office manager.

Fetrow attended Camp Hill public schools through twelfth grade, Albright College for her bachelor's degree (Biochemistry), and Penn State College of Medicine for a Ph.D. (Biological Chemistry), which she earned in 1986 working with George D. Rose. [6] [7] She did post-doctoral stints at the University of Rochester School of Medicine under the mentorship of Fred Sherman, and at the Whitehead Institute at Massachusetts Institute of Technology under the tutelage of Peter S. Kim.

Career

Fetrow worked at the University at Albany, SUNY, from 1990 to 1998, serving as assistant and then associate professor of biological sciences. She then accepted a position at The Scripps Research Institute. Technology that she helped develop at Scripps served as the foundation for GeneFormatics, Inc., the company that Fetrow co-founded and at which she served as Chief Scientific Officer and Director. [8] In August 2003 she was appointed Reynolds Professor of Computational Biophysics at Wake Forest University in the departments of Physics and Computer Science, and in January 2009 she was appointed as Dean of Wake Forest College. She moved to the University of Richmond to serve as Provost and Vice President of Academic Affairs at the University of Richmond in 2014.

In 2017 Fetrow was appointed president of her alma mater, Albright College. [9] Near the end of her initial five-year term the Albright board unanimously approved an additional five-year contract extension. [10] During her time as president, Albright's reputation and stature grew such that it reached #146 in the US News & World Report National Liberal Arts College rankings in 2023, up from 'uncategorized' (below #200) when she began her term as president. [11] She led the drive to right-size Albright's tuition structure in order to be more transparent and to align better with the higher-education market in Pennsylvania and the socioeconomic realities experienced by the college-age student population. [12] At the same time she led the establishment of the Advancing Lives Scholarships endowment to reduce the tuition gap experienced by returning sophomore, junior, and senior students. [13]

As part of efforts to diversify Albright's revenue streams, Fetrow brought to Albright's campus the highly regarded K-12 STEM spectrum of educational programming, originally called Science Research Institute, which has evolved into Total Experience Learning [14] [15] [16] and has been recognized by the United Nations. [17] She worked to bolster Albright's strategic vision as an anchor institution in the city of Reading by transitioning the college's Northeast Reading neighborhood into the Innovation Corridor, a destination and a community where residents live, work, learn and play. [18] Local, state and federal governments provided significant support for the development of that vision. [19] [20] [21] [22] [23] Using external funding, Albright installed the first public electric vehicle charging stations in the city of Reading in 2021. [24]

In April 2024, the Albright College faculty passed a vote of no confidence against President Fetrow. [25] In May 2024, Albright board chair Ron Scheese announced that Fetrow would step down from the presidency, effective May 31, 2024. [26]

Research

Fetrow was the first to describe the non-regular protein structure, omega loop, a structure she identified and studied for her doctoral dissertation (work published under the name Jacquelyn F. Leszczynski). [27] Her early research work involved the experimental analysis of these structures in the protein cytochrome c. [28] [29] [30]

Later, Fetrow's work turned to the classification of functional sites in protein structures, resulting in Fuzzy Functional Forms [31] and active site profiling. [32] This work formed the foundation for the company she co-founded, GeneFormatics. Subsequent development of the active site profiling technology [33] [34] was used to create the Peroxiredoxin Classification Index. [35] [36] [37] This technology has been used to cluster other superfamilies, including the enolases, [38] peroxiredoxins, [37] cytochrome P450s, [39] and arsenate reductases, [40] into functionally relevant clusters.

Awards and honors

Patents awarded

Selected publications

Related Research Articles

<span class="mw-page-title-main">Cytochrome c</span> Protein-coding gene in the species Homo sapiens

The cytochrome complex, or cyt c, is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion where it plays a critical role in cellular respiration. It transfers electrons between Complexes III and IV. Cytochrome c is highly water-soluble, unlike other cytochromes. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It also plays a major role in cell apoptosis. In humans, cytochrome c is encoded by the CYCS gene.

<span class="mw-page-title-main">Structural genomics</span>

Structural genomics seeks to describe the 3-dimensional structure of every protein encoded by a given genome. This genome-based approach allows for a high-throughput method of structure determination by a combination of experimental and modeling approaches. The principal difference between structural genomics and traditional structural prediction is that structural genomics attempts to determine the structure of every protein encoded by the genome, rather than focusing on one particular protein. With full-genome sequences available, structure prediction can be done more quickly through a combination of experimental and modeling approaches, especially because the availability of large number of sequenced genomes and previously solved protein structures allows scientists to model protein structure on the structures of previously solved homologs.

<span class="mw-page-title-main">Plastocyanin</span>

Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it participates in photosynthesis. The protein is a prototype of the blue copper proteins, a family of intensely blue-colored metalloproteins. Specifically, it falls into the group of small type I blue copper proteins called "cupredoxins".

<span class="mw-page-title-main">Protein family</span> Group of evolutionarily-related proteins

A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy.

<span class="mw-page-title-main">Rieske protein</span> Protein family with an iron–sulfur center transferring electrons

Rieske proteins are iron–sulfur protein (ISP) components of cytochrome bc1 complexes and cytochrome b6f complexes and are responsible for electron transfer in some biological systems. John S. Rieske and co-workers first discovered the protein and in 1964 isolated an acetylated form of the bovine mitochondrial protein. In 1979, Trumpower's team isolated the "oxidation factor" from bovine mitochondria and showed it was a reconstitutively-active form of the Rieske iron-sulfur protein
It is a unique [2Fe-2S] cluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV.

<span class="mw-page-title-main">Sulfenic acid</span> Organosulfur compound of the form R–SOH

In chemistry, a sulfenic acid is an organosulfur compound and oxoacid with the general formula R−S−OH. It is the first member of the family of organosulfur oxoacids, which also include sulfinic acids and sulfonic acids, respectively. The base member of the sulfenic acid series with R = H is hydrogen thioperoxide.

The omega loop is a non-regular protein structural motif, consisting of a loop of six or more amino acid residues and any amino acid sequence. The defining characteristic is that residues that make up the beginning and end of the loop are close together in space with no intervening lengths of regular secondary structural motifs. It is named after its shape, which resembles the upper-case Greek letter Omega (Ω).

<span class="mw-page-title-main">21-Hydroxylase</span> Human enzyme that hydroxylates steroids

Steroid 21-hydroxylase is a protein that in humans is encoded by the CYP21A2 gene. The protein is an enzyme that hydroxylates steroids at the C21 position on the molecule. Naming conventions for enzymes are based on the substrate acted upon and the chemical process performed. Biochemically, this enzyme is involved in the biosynthesis of the adrenal gland hormones aldosterone and cortisol, which are important in blood pressure regulation, sodium homeostasis and blood sugar control. The enzyme converts progesterone and 17α-hydroxyprogesterone into 11-deoxycorticosterone and 11-deoxycortisol, respectively, within metabolic pathways which in humans ultimately lead to aldosterone and cortisol creation—deficiency in the enzyme may cause congenital adrenal hyperplasia.

<span class="mw-page-title-main">Peroxiredoxin</span> Family of antioxidant enzymes

Peroxiredoxins are a ubiquitous family of antioxidant enzymes that also control cytokine-induced peroxide levels and thereby mediate signal transduction in mammalian cells. The family members in humans are PRDX1, PRDX2, PRDX3, PRDX4, PRDX5, and PRDX6. The physiological importance of peroxiredoxins is indicated by their relative abundance. Their function is the reduction of peroxides, specifically hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite.

<span class="mw-page-title-main">Cytochrome c family</span> Protein family

Cytochromes c cytochromes, or heme-containing proteins, that have heme C covalently attached to the peptide backbone via one or two thioether bonds. These bonds are in most cases part of a specific Cys-X-X-Cys-His (CXXCH) binding motif, where X denotes a miscellaneous amino acid. Two thioether bonds of cysteine residues bind to the vinyl sidechains of heme, and the histidine residue coordinates one axial binding site of the heme iron. Less common binding motifs can include a single thioether linkage, a lysine or a methionine instead of the axial histidine or a CXnCH binding motif with n>2. The second axial site of the iron can be coordinated by amino acids of the protein, substrate molecules or water. Cytochromes c possess a wide range of properties and function as electron transfer proteins or catalyse chemical reactions involving redox processes. A prominent member of this family is mitochondrial cytochrome c.

<span class="mw-page-title-main">CYP3A5</span> Enzyme involved in drug metabolism

Cytochrome P450 3A5 is a protein that in humans is encoded by the CYP3A5 gene.

<span class="mw-page-title-main">Peroxiredoxin 1</span> Protein found in humans

Peroxiredoxin-1 is a protein that in humans is encoded by the PRDX1 gene.

<span class="mw-page-title-main">Peroxiredoxin 2</span> Protein found in humans

Peroxiredoxin-2 is a protein that in humans is encoded by the PRDX2 gene.

<span class="mw-page-title-main">PRDX6</span> Protein-coding gene in the species Homo sapiens

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene. It is a member of the peroxiredoxin family of antioxidant enzymes.

<span class="mw-page-title-main">PRDX5</span> Protein-coding gene in the species Homo sapiens

Peroxiredoxin-5 (PRDX5), mitochondrial is a protein that in humans is encoded by the PRDX5 gene, located on chromosome 11.

<span class="mw-page-title-main">CYP4F2</span> Enzyme protein in the species Homo sapiens

Cytochrome P450 4F2 is a protein that in humans is encoded by the CYP4F2 gene. This protein is an enzyme, a type of protein that catalyzes chemical reactions inside cells. This specific enzyme is part of the superfamily of cytochrome P450 (CYP) enzymes, and the encoding gene is part of a cluster of cytochrome P450 genes located on chromosome 19.

Protein function prediction methods are techniques that bioinformatics researchers use to assign biological or biochemical roles to proteins. These proteins are usually ones that are poorly studied or predicted based on genomic sequence data. These predictions are often driven by data-intensive computational procedures. Information may come from nucleic acid sequence homology, gene expression profiles, protein domain structures, text mining of publications, phylogenetic profiles, phenotypic profiles, and protein-protein interaction. Protein function is a broad term: the roles of proteins range from catalysis of biochemical reactions to transport to signal transduction, and a single protein may play a role in multiple processes or cellular pathways.

PeroxiRedoxin classification indEX (PREX) is a database of peroxiredoxins (Prxs) classified into one of six distinct subfamilies. Classification relies on the Deacon Active Site Profiling (DASP) approach that utilizes a position specific scoring matrix (PSSM) created from aligned signatures to search sequence databases. Searches of PREX for Prxs of interest can be conducted using protein annotation, accession number, PDB ID, organism name, or protein sequence for Prx proteins extracted from January 2008, November 2010, or October 2011 versions of GenBank. Output includes the subfamily to which each classified Prx belongs, accession and GI numbers, genus and species, and the active site signature used for classification. The query sequence is also presented aligned with a select group of Prxs for manual evaluation and interpretation by the user. This resource is freely available to the research community.

<span class="mw-page-title-main">I-TASSER</span>

I-TASSER is a bioinformatics method for predicting three-dimensional structure model of protein molecules from amino acid sequences. It detects structure templates from the Protein Data Bank by a technique called fold recognition. The full-length structure models are constructed by reassembling structural fragments from threading templates using replica exchange Monte Carlo simulations. I-TASSER is one of the most successful protein structure prediction methods in the community-wide CASP experiments.

Jeffrey Skolnick is an American computational biologist. He is currently a Georgia Institute of Technology School of Biology Professor, the Director of the Center for the Study of Systems Biology, the Mary and Maisie Gibson Chair, the Georgia Research Alliance Eminent Scholar in Computational Systems Biology, the Director of the Integrative BioSystems Institute, and was previously the Scientific Advisor at Intellimedix.

References

  1. ↑ "Albright College Names Alumna Jacquelyn S. Fetrow as Its 15th President | Albright College". Albright College. 2016-10-28. Retrieved 2018-03-07.
  2. ↑ "University of Richmond News". news.richmond.edu. Retrieved 2018-03-07.
  3. ↑ "Dean of the College | Inside Higher Ed". insidehighered.com. Retrieved 2018-03-07.
  4. ↑ "Camp Hill native to lead Albright College in 2017". PennLive.com. Retrieved 2018-03-07.
  5. ↑ "Mildred F. "Millie" Fetrow's Obituary on Patriot-News". Patriot-News. Retrieved 2018-03-07.
  6. ↑ "George D. Rose". Johns Hopkins University. 3 June 2016.
  7. ↑ "New Albright president sworn in | Reading Eagle - NEWS". Reading Eagle. Retrieved 2018-03-07.
  8. ↑ "The Business of Biotech". www.albright.edu. Retrieved 2018-03-07.
  9. ↑ "Alumna Jacquelyn S. Fetrow Named 15th President of Albright College". Albright College News. 2016-10-28. Retrieved 2024-06-09.
  10. ↑ Adams, Heather (2022-09-02). "Albright Board Unanimously Votes to Extend President Fetrow's Contract". BCTV. Retrieved 2024-06-09.
  11. ↑ "Albright College - Profile, Rankings and Data". US News Best Colleges. Retrieved May 29, 2024.
  12. ↑ "Albright College to 'right-size' tuition". Berks Regional News | WFMZ.com. 2019-01-14. Retrieved 2024-05-29.
  13. ↑ "Advancing Lives Scholarship". Albright College. Retrieved 2024-05-29.
  14. ↑ "Science Research Institute expands to Albright College". Berks Regional News | WFMZ.com. 2020-02-07. Retrieved 2024-05-29.
  15. ↑ "Total Experience Learning". Albright College. Retrieved 2024-05-29.
  16. ↑ Tom, Rader (2022-02-17). "Albright College Science Research Institute_3". WFMZ.com. Retrieved 2024-05-29.
  17. ↑ Mekeel, David (2023-01-25). "Albright College's Total Experience Learning institute is getting international attention". Reading Eagle. Retrieved 2024-05-29.
  18. ↑ Gonzalez, Lexi (2024-03-26). "Spotlight on Innovation Corridor in Northeast Reading". BCTV. Retrieved 2024-05-29.
  19. ↑ Griffaton, Grace (2022-11-15). "Albright College details plans for $3 million state grant". WFMZ.com. Retrieved 2024-05-29.
  20. ↑ Kostival, David (2022-11-21). "Albright, Alvernia, RACC could each get $2M from Reading". WFMZ.com. Retrieved 2024-05-29.
  21. ↑ Kostival, David (2023-06-22). "Berks County Commissioners authorize financing resolution for Albright College". WFMZ.com. Retrieved 2024-05-29.
  22. ↑ Lynch, Michelle (2024-01-22). "State official tours northeast Reading area targeted for revitalization by Habitat for Humanity of Berks County". Reading Eagle. Retrieved 2024-05-29.
  23. ↑ "Houlahan secures $11.7M for 14 community organizations". Berks Weekly. 2024-03-15. Retrieved 2024-05-29.
  24. ↑ Kolodziej, Ellen (2021-12-10). "Albright College is adding electric charging stations". WFMZ.com. Retrieved 2024-05-29.
  25. ↑ "Faculty votes no-confidence in Albright College president, provost". 25 April 2024.
  26. ↑ "Albright College president Jacquelyn Fetrow resigns". 14 May 2024.
  27. 1 2 Leszczynski JF, Rose GD (November 1986). "Loops in globular proteins: a novel category of secondary structure". Science. 234 (4778): 849–55. Bibcode:1986Sci...234..849L. doi:10.1126/science.3775366. PMID   3775366.
  28. ↑ Fetrow JS, Cardillo TS, Sherman F (1989). "Deletions and replacements of omega loops in yeast iso-1-cytochrome c". Proteins. 6 (4): 372–81. doi:10.1002/prot.340060404. PMID   2560195. S2CID   25525703.
  29. ↑ Murphy ME, Fetrow JS, Burton RE, Brayer GD (September 1993). "The structure and function of omega loop A replacements in cytochrome c". Protein Science. 2 (9): 1429–40. doi:10.1002/pro.5560020907. PMC   2142463 . PMID   8401228.
  30. ↑ Mulligan-Pullyblank P, Spitzer JS, Gilden BM, Fetrow JS (April 1996). "Loop replacement and random mutagenesis of omega-loop D, residues 70-84, in iso-1-cytochrome c". The Journal of Biological Chemistry. 271 (15): 8633–45. doi: 10.1074/jbc.271.15.8633 . PMID   8621494.
  31. 1 2 Fetrow JS, Skolnick J (September 1998). "Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases". Journal of Molecular Biology. 281 (5): 949–68. doi:10.1006/jmbi.1998.1993. PMID   9719646.
  32. 1 2 Cammer SA, Hoffman BT, Speir JA, Canady MA, Nelson MR, Knutson S, Gallina M, Baxter SM, Fetrow JS (November 2003). "Structure-based active site profiles for genome analysis and functional family subclassification". Journal of Molecular Biology. 334 (3): 387–401. doi:10.1016/j.jmb.2003.09.062. PMID   14623182.
  33. ↑ Huff RG, Bayram E, Tan H, Knutson ST, Knaggs MH, Richon AB, Santago P, Fetrow JS (November 2005). "Chemical and structural diversity in cyclooxygenase protein active sites". Chemistry & Biodiversity. 2 (11): 1533–52. doi:10.1002/cbdv.200590125. hdl: 10339/16028 . PMID   17191953. S2CID   25066310.
  34. ↑ Fetrow JS (July 2006). Active site profiling to identify protein functional sites in sequences and structures using the Deacon Active Site Profiler (DASP). Vol. Chapter 8. pp. 8.10.1–8.10.16. doi:10.1002/0471250953.bi0810s14. ISBN   978-0471250951. PMID   18428769.{{cite book}}: |journal= ignored (help)
  35. ↑ Soito L, Williamson C, Knutson ST, Fetrow JS, Poole LB, Nelson KJ (January 2011). "PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family". Nucleic Acids Research. 39 (Database issue): D332–7. doi:10.1093/nar/gkq1060. PMC   3013668 . PMID   21036863.
  36. ↑ Nelson KJ, Knutson ST, Soito L, Klomsiri C, Poole LB, Fetrow JS (March 2011). "Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis". Proteins. 79 (3): 947–64. doi:10.1002/prot.22936. PMC   3065352 . PMID   21287625.
  37. 1 2 3 Harper AF, Leuthaeuser JB, Babbitt PC, Morris JH, Ferrin TE, Poole LB, Fetrow JS (February 2017). "An Atlas of Peroxiredoxins Created Using an Active Site Profile-Based Approach to Functionally Relevant Clustering of Proteins". PLOS Computational Biology. 13 (2): e1005284. Bibcode:2017PLSCB..13E5284H. doi: 10.1371/journal.pcbi.1005284 . PMC   5302317 . PMID   28187133.
  38. ↑ Knutson ST, Westwood BM, Leuthaeuser JB, Turner BE, Nguyendac D, Shea G, Kumar K, Hayden JD, Harper AF, Brown SD, Morris JH, Ferrin TE, Babbitt PC, Fetrow JS (April 2017). "An approach to functionally relevant clustering of the protein universe: Active site profile-based clustering of protein structures and sequences". Protein Science. 26 (4): 677–699. doi:10.1002/pro.3112. PMC   5368075 . PMID   28054422.
  39. 1 2 Gober JG, Rydeen AE, Gibson-O'Grady EJ, Leuthaeuser JB, Fetrow JS, Brustad EM (March 2, 2016). "Mutating a Highly Conserved Residue in Diverse Cytochrome P450s Facilitates Diastereoselective Olefin Cyclopropanation". ChemBioChem. 17 (5): 394–397. doi:10.1002/cbic.201500624. PMC   5241096 . PMID   26690878.
  40. 1 2 Rosen MR, Leuthaeuser JB, Parish CA, Fetrow JS (November 2, 2020). "Isofunctional Clustering and Conformational Analysis of the Arsenate Reductase Superfamily Reveals Nine Distinct Clusters". Biochemistry. 59 (44): 4262–4284. doi:10.1021/acs.biochem.0c00651. PMID   33135415. S2CID   226233138.
  41. ↑ "19 Penn Staters honored with Alumni Fellow Award | Penn State University" . Retrieved 2018-03-07.
  42. 1 2 "Alumni Awards | Albright College". Albright College. Retrieved 2018-03-07.
  43. ↑ "Faculty Awards". www.albany.edu. Retrieved 2018-03-07.
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