Harold Scheraga

Harold Scheraga
Born (1921-10-18)October 18, 1921
Brooklyn, New York
Citizenship American
Fields biophysics
Institutions Cornell University
Education Duke University
Known for Theoretical and computational studies of protein folding

Harold Scheraga (born 1921) is an American biophysicist, currently the George W. and Grace L. Todd Professor Emeritus in the chemistry department at Cornell University.[1] Scheraga is regarded as a pioneer in protein biophysics and has been especially influential in the study of protein solvation and the hydrophobic effect as it relates to protein folding.[2]

Early life and education

Scheraga was born in 1921 in Brooklyn, New York and spent his early life in Monticello, New York. His father worked as a machinist and opened a business there. The family returned to Brooklyn in 1929 due to business losses following the 1929 Wall Street Crash and struggled economically through the Great Depression. As a high school student, Scheraga was interested in mathematics and especially in classics, which he intended to pursue in college, but exposure to physics during his education at the City College of New York convinced him to focus on physical chemistry.[3] He received his bachelor's degree from CCNY in 1941 and his Ph.D. from Duke University in 1946.[1] During his graduate work, he spent time on projects related to the US war effort in World War II as well as on his own research. While at Duke he worked with Fritz London, Paul Gross, and others.[3] After graduation he spent a year as a postdoctoral fellow at Harvard Medical School with John Edsall, where he first began to work with proteins.[3]

Academic career

Scheraga has spent his entire academic career at Cornell University, beginning with an appointment as an instructor in 1947, becoming an associate professor in 1950, and eventually being promoted to full professor in 1958. As he later recalled, he was offered the instructor appointment by Peter Debye on the same day as his interview.[3] He became the Todd Professor of Chemistry in 1965 and retired, assuming emeritus status, in 1992. Scheraga served as the department chair from 1960-67.[1] Throughout his faculty career, Scheraga taught undergraduate courses in physical chemistry, as well as graduate courses focused more specifically on proteins.[3]

Research

Scheraga's research career has focused on protein biophysics, beginning in the 1940s when little was known about the subject. His work on protein solvation, the hydrophobic effect, and the consequences for protein folding was controversial in its early stages, but has been highly influential. He has also been a significant contributor in theoretical and computational biophysics, developing statistical mechanical models for the hydrophobic effect and playing a key role in early molecular mechanics models of proteins, developing force fields for use in protein and peptide simulations.[2] Most of his more recent work has focused on molecular dynamics simulations of proteins and protein folding, particularly as compared to NMR measurements.[3][4]

Personal life

Scheraga met his wife Miriam Kernow, at the time a sociology student at Brooklyn College, through a Jewish social club in Brooklyn in which he participated during his time as a CCNY student. They married while Scheraga was at Duke, where Miriam briefly took a technician job in analytical chemistry to support the couple. She later worked in the Cornell University library. They have three children.[3]

Awards and honors

Scheraga has received numerous awards in recognition of his influence in the protein biophysics field.[1]

References

  1. 1 2 3 4 "Scheraga Group Homepage". Cornell University. Retrieved 16 December 2015.
  2. 1 2 Hammes, GG; Skolnick, J (14 June 2012). "Career accomplishments of Harold A. Scheraga.". The journal of physical chemistry. B 116 (23): 6569–71. PMID 22697899.
  3. 1 2 3 4 5 6 7 Scheraga, HA (2011). "Respice, adspice, and prospice.". Annual Review of Biophysics 40: 1–39. PMID 21545283.
  4. Scheraga, HA (May 2015). "My 65 years in protein chemistry.". Quarterly reviews of biophysics 48 (2): 117–77. doi:10.1017/S0033583514000134. PMID 25850343.
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