User:Eric Martz/Introduction to Structural Bioinformatics I: Difference between revisions
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::A. Although sequence specifies fold, scientists '''cannot yet predict the fold from the sequence'''. Therefore, fold must be determined by empirical (experimental) methods. The most common methods for determining the 3D structure of a protein molecule are: | ::A. Although sequence specifies fold, scientists '''cannot yet predict the fold from the sequence'''. Therefore, fold must be determined by empirical (experimental) methods. The most common methods for determining the 3D structure of a protein molecule are: | ||
:::*[[X-ray crystallography]], 88%. | :::*[[X-ray crystallography]], 88%. | ||
::::Cannot determine the structure of [[Intrinsically Disordered Protein|intrinsically unstructured]] loops or molecules. | ::::*Cannot determine the structure of [[Intrinsically Disordered Protein|intrinsically unstructured]] loops or molecules. | ||
::::*Result is a single model representing the average of the molecules in the crystal. | |||
::::*[[Resolution]] reflects the degree of order or disorder in the crystal. | |||
:::*[[Nuclear magnetic resonance]] (NMR) in aqueous solution, 11%. | :::*[[Nuclear magnetic resonance]] (NMR) in aqueous solution, 11%. | ||
::::*NMR is limited to small proteins (30 kD or smaller). | ::::*NMR is limited to small proteins (30 kD or smaller). | ||
::::*Result is an ensemble of models consistent with the data. Examples: [[2bbn]] | |||
:::*High resolution cryo-electron microscopy, 0.5%. | :::*High resolution cryo-electron microscopy, 0.5%. | ||