Alexander Rich

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Alexander Rich
Born (1924-11-15) 15 November 1924 (age 90)
Hartford, Connecticut, USA
Residence Cambridge, Massachusetts, USA
Nationality USA
Fields Biophysics
Institutions Massachusetts Institute of Technology
Alma mater Harvard University, USA
Known for discoverer of polysomes and Z-DNA
Influences Francis Crick[1]
Notable awards

Alexander Rich, MD (American; born 15 November 1924 in Hartford, Connecticut[2]) is a biologist and biophysicist. He is the William Thompson Sedgwick Professor of Biophysics at MIT (since 1958) and Harvard Medical School. Dr. Rich earned both an A.B. (magna cum laude) and an M.D. (cum laude) from Harvard University. He was a post-doc of Linus Pauling along with James Watson. He has over 600 publications to his name.

Rich is married to Jane Erving Rich and they have four children: Benjamin E., Josiah D., Rebecca B., and Jessica J.[2]

Rich is the founder of Alkermes and has been its director since 1987. Dr. Rich is Co-Chairman of the Board of Directors of Repligen Corporation, a biopharmaceutical company. He is also a member of the Board of Directors for Profectus BioSciences, Inc. He also serves on the editorial board of Genomics and the Journal of Biomolecular Structure and Dynamics.

In 1963, Rich discovered polysomes: clusters of ribosomes which read one strand of mRNA simultaneously.[3]

In 1979, Rich and co-workers at MIT grew a crystal of Z-DNA.[4] This was the first crystal structure of any form of DNA. After 26 years of attempts, Rich et al. finally crystallised the junction box of B- and Z-DNA. Their results were published in an October 2005 Nature journal.[5] Whenever Z-DNA forms, there must be two junction boxes that allow the flip back to the canonical B-form of DNA.

List of awards and prizes received[edit]

Awards and prizes[edit]

  • Sigma Xi Proctor Prize, Raleigh, NC (2001)
  • Bower Award and Prize, the Franklin Institute, Philadelphia, PA (2000)
  • National Medal of Science, Washington, DC (1995)
  • Linus Pauling Medal, American Chemical Society, Northwest Sections (1995)
  • Lewis S. Rosenstiel Award in Basic Biomedical Research, Brandeis Univ., Waltham, MA (1983)
  • James R. Killian Faculty Achievement Award, Massachusetts Institute of Technology (1980)
  • Presidential Award, New York Academy of Science, New York, NY (1977)
  • Theodore van Karmen Award for Viking Mars Mission, Washington, DC (1976)
  • Skylab Achievement Award, National Aeronautics and Space Administration, Washington, DC (1974)


  • Foreign Member, Russian Academy of Sciences, Moscow, Russia (1994)
  • Honorary Member, Japanese Biochemical Society, Tokyo, Japan (1986)
  • Foreign Member, French Academy of Sciences, Paris, France (1984)
  • Honorary Doctorate, Federal University of Rio de Janeiro, Brazil (1981)
  • American Philosophical Society, Philadelphia, PA (1980)
  • Pontifical Academy of Sciences (1978)
  • National Academy of Sciences, Washington, DC (1970)
  • Fellow, American Association for the Advancement of Science, Washington, DC (1965)
  • Fellow, Guggenheim Foundation (1963)
  • Fellow, American Academy of Arts and Sciences, Boston, MA (1959)
  • Fellow, National Research Council, Washington, DC (1949-51).


  1. ^ Rich, A.; Stevens, C. F. (2004). "Obituary: Francis Crick (1916–2004)". Nature 430 (7002): 845–847. doi:10.1038/430845a. PMID 15318208. 
  2. ^ a b c
  3. ^ Warner JR, Knopf PM, Rich A (1963). "A MULTIPLE RIBOSOMAL STRUCTURE IN PROTEIN SYNTHESIS". Proceedings of the National Academy of Sciences of the United States of America 49 (1): 122–129. Bibcode:1963PNAS...49..122W. doi:10.1073/pnas.49.1.122. PMC 300639. PMID 13998950. 
  4. ^ Wang AHJ, Quigley GJ, Kolpak FJ, Crawford JL, van Boom JH, Van der Marel G, and Rich A (1979). "Molecular structure of a left-handed double helical DNA fragment at atomic resolution". Nature 282 (5740): 680–686. Bibcode:1979Natur.282..680W. doi:10.1038/282680a0. PMID 514347. 
  5. ^ Ha SC, Lowenhaupt K, Rich A, Kim YG, and Kim KK (2005). "Crystal structure of a junction between B-DNA and Z-DNA reveals two extruded bases". Nature 437 (7062): 1183–1186. Bibcode:2005Natur.437.1183H. doi:10.1038/nature04088. PMID 16237447. 
  6. ^ "2008 Welch Award in Chemistry Recipient". The Welch Foundation. 

Selected publications[edit]

  • Brown BA II, Lowenhaupt K, Wilbert CM, Hanlon EB, Rich A (2000). "The Za domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA". Proceedings of the National Academy of Sciences of the United States of America 97 (25): 13531–13586. Bibcode:2000PNAS...9713532B. doi:10.1073/pnas.240464097. JSTOR 2666404. 
  • Kim Y-G, Lowenhaupt K, Maas S, Herbert A, Schwartz T, Rich A (2000). "The Zab domain of the human RNA editing enzyme ADAR1 recognizes Z-DNA when surrounded by B-DNA". J Biol Chem 275 (35): 26828–26833. doi:10.1074/jbc.M003477200. PMID 10843996. 
  • Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A (1999). "Crystal structure of the Za domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA". Science 284 (5421): 1841–1845. doi:10.1126/science.284.5421.1841. PMID 10364558. 

External links[edit]