BIOC 2580 Lecture 10: Day 10: States of proteins [Jan 30]
10 Feb 2017
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Often irreversible a protein"s function is typically lost on denaturation. Ways to denature proteins include: heat disruptive solvents harsh detergents (i. e. sds) Day 10: states of proteins [jan 30] protein structure is organized in three (or four) levels native and denatured states of proteins. Most proteins are folded into a unique 3d tertiary structure, which is required for their function native state denaturation unfolds proteins; unfolded form may be unstructured or aggregated. When purifying proteins to study them, we usually try to avoid denaturation tertiary structure is the overall pattern of folding of the whole polypeptide chain the simplest possible tertiary structure is continuous secondary structure. Most proteins are globular: this requires the polypeptide to fold back on itself folding requires breaks" in secondary structure, which is rigid clusters of 2-3 secondary structure breakers (gly, pro, asn, asp, or ser; Aas that prefer -sheet are present, but scattered.
