ISSN:
1476-4687
Source:
Nature Archives 1869 - 2009
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
Notes:
[Auszug] Each subunit of triose phosphate isomerase is composed of alternate segments of polypeptide chain in the α- and β-conformations that are arranged to form an inner cylinder of parallel-pleated sheet and a largely helical outer shell. Residues participating in the subunit interface and the ...
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1038/255609a0
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