User:Eric Martz/Introduction to Structural Bioinformatics I: Difference between revisions
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==II. Protein Structure and Structural Bioinformatics== | ==II. Protein Structure and Structural Bioinformatics== | ||
:<span style="font-size:130%">1. [[Amino acid]] '''sequence''' + protein chain '''conformation''' = protein '''function'''.</span> | :<span style="font-size:130%">1. [[Amino acid]] '''sequence''' + protein chain '''conformation''' = protein '''function'''.</span> | ||
::A. Conformation can be a '''stable fold''' or '''[[Intrinsically Disordered Protein|intrinsically unstructured]]'''. Both commonly exist in the same protein molecule. | ::A. [http://www.umass.edu/molvis/workshop/allstruc/whycare.htm Why do we care?] | ||
:: | ::B. Conformation can be a '''stable fold''' or '''[[Intrinsically Disordered Protein|intrinsically unstructured]]'''. Both commonly exist in the same protein molecule. | ||
::C. Conformation is specified by sequence. | |||
:::*Folded domains fold spontaneously (Anfinson, 1960's<ref>For a brief overview of Anfinson's protein folding experiments in the 1960's, see the first paragraph at [[Intrinsically Disordered Protein]].</ref>), or with the help of [[chaperonins]]. | :::*Folded domains fold spontaneously (Anfinson, 1960's<ref>For a brief overview of Anfinson's protein folding experiments in the 1960's, 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. | ||
