Author(s):  
Mark Lorch

This chapter traces the history of biochemistry, which is linked to the understanding of arguably the oldest uses of biotechnology—fermentation and the production of alcoholic beverages and cheese. In the 19th century, at the same time as the fermentation debates and enzymology flourished, the nature of proteins was under scrutiny. The chapter then considers the contribution that X-ray crystallography has made to structural biology. By the mid-20th century, the structures of the two massive molecular players, protein and nucleic acids (DNA along with ribonucleic acid), and their myriad roles were in place. It was becoming apparent that these were the fundamental molecular machines that marshal the chemistry within cells.


2007 ◽  
Vol 362 (1482) ◽  
pp. 1035-1042 ◽  
Author(s):  
Zihe Rao

China has a strong background in X-ray crystallography dating back to the 1920s. Protein crystallography research in China was first developed following the successful synthesis of insulin in China in 1966. The subsequent determination of the three-dimensional structure of porcine insulin made China one of the few countries which could determine macromolecular structures by X-ray diffraction methods in the late 1960s and early 1970s. After a slow period during the 1970s and 1980s, protein crystallography in China has reached a new climax with a number of outstanding accomplishments. Here, I review the history and progress of protein crystallography in China and detail some of the recent research highlights, including the crystal structures of two membrane proteins as well as the structural genomics initiative in China.


2017 ◽  
Vol 47 (3) ◽  
pp. 389-422 ◽  
Author(s):  
Carsten Reinhardt

Nuclear magnetic resonance (NMR) spectroscopy has been and continues to be one of the most widely spread research techniques in the physical and life sciences, including medicine, since the technique’s invention in 1945. There is no basis, however, to account for a linear success story. Although NMR was used for decades in biochemistry and molecular biology, it had not contributed substantially to solving the big scientific problems in these areas. The goal set by its early proponents—to find out about the dynamics and functions of large biomolecules—was not successfully tackled until the 1980s, when new technology became available. Much of the pre-1980s history of NMR is arguably a history of the dependence of NMR on a rival method, x-ray crystallography. In this paper I will discuss the epistemic and social processes that made the continuation of NMR as a dependent research method possible, perhaps even inevitable. Following a comparison of x-ray crystallography and NMR in the structural elucidation of large biomolecules, the paper analyzes three examples of the practices of biochemical and biomedical research using NMR from the 1950s to the 1970s in the United States: first is a fundamental, almost reductionist approach with a basis in physics and goals in technology; second, a pragmatic one with a strong bent toward biological problems; and third, a methods-oriented program, involving issues of the former two and proving the most fruitful in the long term. This essay is part of a special issue entitled THE BONDS OF HISTORY edited by Anita Guerrini.


DNA Repair ◽  
2020 ◽  
Vol 93 ◽  
pp. 102928 ◽  
Author(s):  
Amy M. Whitaker ◽  
Bret D. Freudenthal

1990 ◽  
Vol 1 (6) ◽  
pp. 617-620 ◽  
Author(s):  
Herbert A. Hauptman

Genetics ◽  
2000 ◽  
Vol 154 (1) ◽  
pp. 27-37
Author(s):  
W D Crill ◽  
H A Wichman ◽  
J J Bull

Abstract Experimental adaptation of the bacteriophage ϕX174 to a Salmonella host depressed its ability to grow on the traditional Escherichia host, whereas adaptation to Escherichia did not appreciably affect growth on Salmonella. Continued host switching consistently exhibited this pattern. Growth inhibition on Escherichia resulted from two to three substitutions in the major capsid gene. When these phages were forced to grow again on Escherichia, fitness recovery occurred predominantly by reversions at these same sites, rather than by second-site compensatory changes, the more frequently observed mechanism in most microbial systems. The affected residues lie on the virion surface and they alter attachment efficiency, yet they occur in a region distinct from a putative binding region previously identified from X-ray crystallography. These residues not only experienced high rates of evolution in our experiments, but also exhibited high levels of radical amino acid variation among ϕX174 and its known relatives, consistent with a history of adaptation involving these sites.


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