Monday, January 29, 2007

Monday, January 29, 2007 - Stabilizing tertiary structure...

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Stabilizing tertiary structure Weak Hydrogen bonds Ionic interactions Hydrophobic and van der waals interactions. Strong Disulfide bridge (covalent bond) Disulfide bridges SH groups of two cysteines form covalent bonds. Quaternary Structure Multiple poplypeptide chains (subunits) fit together to form a larger protein Can be identical subunits or different polypeptide chains. Native and denatured proteins Native – properly folded and functional (3 dimensional shape) Denature – unfolded and does not function Roles of Weak bonds in biological systems Weak bonds are easily made and broken at physiological temperatures Weak bonds provide specificity. If “weak” interactions were “strong”, it would crystallize the contents of a cell. Weak bonds attrack and attach substrates to enzymes. Weak bonds determine molecular shape = a compromise between backbone and side groups.
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Monday, January 29, 2007 - Stabilizing tertiary structure...

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