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Lecture

BIOCH 200 (February 7, 2014) - Protein Structure and Function

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Department
Biochemistry
Course
BIOCH200
Professor
Walter Dixon
Semester
Winter

Description
BIOCH 200: Protein Structure and Function (February 7, 2014) • *It is the hydrophobic interaction that occur within a globular protein that give it its 3D shape o *The hydrophobic parts are more inclined to be present at the center of the protein o *The hydrophilic parts are more inclined to be present on the outside of the protein o *In fact, the shape of a globular protein is greatly dictated by where the hydrophobic segments of the polypeptide strand is (primary structure)  *Structure shape is more fine-tuned via hydrogen bonding, ion pairs (electrostatic interactions), and disulphide bridges (covalent bonds found in Cysteine dimers) • *In β-sheet proteins, the loops that connect the sheets tend to face outside where they have a higher chance to participate in h-bonding with other molecules • Extra information from I-Clicker Questions in Class: o Glycine and Valine never get ionized no matter the pH o *NOTE THAT: A charged amino acid is not synonymous same as an amino acid with a charged R-group *Domain – segment in a polypeptide that has folded into a single FUNCTIONAL unit w/ a hydrophobic core (aka – “functional subregions withi
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