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Protein Crystal Growth in Microgravity
Author(s) -
Bugg Charles E.,
DeLucas Lawrence J.
Publication year - 1991
Publication title -
the journal of clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.92
H-Index - 116
eISSN - 1552-4604
pISSN - 0091-2700
DOI - 10.1002/j.1552-4604.1991.tb03660.x
Subject(s) - macromolecule , nucleic acid , macromolecular substances , function (biology) , chemistry , protein crystallization , protein structure , computational biology , crystallography , biochemistry , biology , crystallization , genetics , organic chemistry
Protein crystallography is a powerful method for determining the three‐dimensional structures of biological macromolecules. Although new methods, such as two‐dimensional NMR, have demonstrated promise for determining the structures of small proteins and nucleic acids, the complete atomic arrangements within large proteins can only be determined at present using crystallographic techniques. Such crystallographic studies have been of major importance for establishing structure/function relationships that are fundamental to understanding how enzymes, nucleic acids, and other macromolecules function in biological systems. More recently, crystallographic studies of proteins have become of considerable practical interest within the pharmaceutical and biotechnology industries, as promising tools in drug design and in protein engineering.