User:Eric Martz/Introduction to Structural Bioinformatics I
From Proteopedia
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::A. Conformation can be a '''stable fold''' or '''[[Intrinsically Disordered Protein|intrinsically unstructured]]'''. Both commonly exist in the same protein molecule. | ::A. Conformation can be a '''stable fold''' or '''[[Intrinsically Disordered Protein|intrinsically unstructured]]'''. Both commonly exist in the same protein molecule. | ||
::B. Conformation is determined by sequence. | ::B. Conformation is determined by sequence. | ||
| - | :::Folded domains fold spontaneously (Anfinson, | + | :::Folded domains fold spontaneously (Anfinson, 1960's<ref>For a brief overview of Anfinson's initial folding experiments, see the first paragraph at [[Intrinsically Disordered Protein]].</ref>), or with the help of [[chaperonins]]. |
:::The '''denaturation''' (unfolding) of a folded domain destroys its function. | :::The '''denaturation''' (unfolding) of a folded domain destroys its function. | ||
Revision as of 21:41, 27 September 2012
How to find, visualize, and understand 3D protein molecular structures
by Eric Martz, October 2 and 4, 2012
for Prof. Steven Sandler's course Microbiology 565: Laboratory in Molecular Genetics
University of Massachusetts, Amherst MA USA
Protein Structure
- 1. Amino acid sequence + protein chain conformation = protein function.
- A. Conformation can be a stable fold or intrinsically unstructured. Both commonly exist in the same protein molecule.
- B. Conformation is determined by sequence.
- Folded domains fold spontaneously (Anfinson, 1960's[1]), or with the help of chaperonins.
- The denaturation (unfolding) of a folded domain destroys its function.
