Open AccessMaterials ScienceMedicineChemistry

C. Bugg, L. DeLucas

1989.11.3JOURNAL OF CLINICAL PHARMACOLOGY

DOI: 10.1126/science.2510297

tlooto Summary

The complete atomic arrangements within large proteins can only be determined at present using crystallographic techniques, and 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.

Abstract

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.

Citation format

BUGG, C.; DELUCAS, L. Protein crystal growth in microgravity. JOURNAL OF CLINICAL PHARMACOLOGY, 1989, 31 10: 985–7.