Biomolecules are too small to see in detail even with the most advanced light microscopes. The methods that structural biologists use to determine their structures generally involve measurements on vast numbers of identical molecules at the same time. These methods include crystallography, NMR, ultra fast laser spectroscopy, electron microscopy, electron cryomicroscopy (cryo-EM), Dual Polarisation Interferometry and circular dichroism. Most often researchers use them to study the static "native states" of macromolecules. But variations on these methods are also used to watch nascent or denatured molecules assume or reassume their native states. See protein folding.
A third approach that structural biologists take to understanding structure is bioinformatics to look for patterns among the diverse sequences that give rise to particular shapes. Researchers often can deduce aspects of the structure of integral membrane proteins based on the membrane topology predicted by hydrophobicity analysis. See protein structure prediction.
In the past few years it has become possible for highly accurate physical molecular models to complement the in silico study of biological structures.
See also
- primary structure
- secondary structure
- tertiary structure
- quaternary structure
- structural domain
- structural motif
- protein subunit
- molecular model
- cooperativity
- chaperonin
- structural genomics
- stereochemistry
- resolution (electron density)
- Proteopedia The collaborative, 3D encyclopedia of proteins and other molecules.
External links
- Nature: Structural & Molecular Biology magazine website
- Structural Biology - The Virtual Library of Biochemistry and Cell Biology
- NCCR Structural Biology - A Swiss research initiative encompassing the structural biology of membrane proteins and supramolecular assemblies
- The Tel Aviv University Structural Biology Lab at The Life Sciences Faculty
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Last updated on Wednesday July 09, 2008 at 05:16:59 PDT (GMT -0700)
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