Notes in d. Protein Stability and Folding

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Published	07/28/2024	{{c1::hydrophobic forces}} are the most important intermolecular force contributing to protein folding.
Published	07/28/2024	Protein denaturing agents include:
Published	07/28/2024	{{c1::Detergenes}} hydrophobically associate with nonpolar side chains, interfering with the hydrophobic interactions responsible for native structure…
Published	07/28/2024	{{c1::Water soluble organic substances}} interfere with hydrophobic forces stabilizing native structures through their own hydrophobic interactions wi…
Published	07/28/2024	{{c1::chaotropic agents}} increase the solubility of nonpolar substances in water, so denature by disrupting hydrophobic interactions (ex: urea, guani…
Published	07/28/2024	What is cooperative folding/unfolding?
Published	07/28/2024	The earliest protein folding events are initiated by {{c1::hydrophobic collapse}}
Published	07/28/2024	Final folding events are relatively slow and often benefit from {{c1::accessory proteins}}
Published	07/28/2024	The three types of accessory proteins that aid in protein folding are:
Published	07/28/2024	{{c1::Protein disulfide isomerase}} functions to re-arrange disulfide bonds either via catalysis or by serving as an oxidizing agent
Published	07/28/2024	Show how Protein disulfide isomerase may function as a catalytic enzyme in rearranging disulfide bonds:
Published	07/28/2024	Show how protein disulfide isomerase may function as an oxidizing agent in the formation of disulfide bonds:
Published	07/28/2024	{{c1::Peptidyl Prolyl cis-trans isomerase (PPI)}} catalyze the interconversion of aa-Pro peptide bonds between cis and trans
Published	07/28/2024	{{c1::Molecular chaperones}} bind to an unfolded polypeptide's exposed hydrophobic surfaces and then releases them, often repeatedly to facilitate fol…
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Published	07/28/2024	Elucidate the mechanism of protein folding for the GroEL/GroES Molecular Chaperone
Published	07/28/2024	Some diseases are associated with the deposition of normally soluble proteins in certain tissues in the form of insoluble aggregates called {{c1:…
Published	07/28/2024	Some examples of disease of protein conformation are {{c1::alzheimer's}} and {{c2::transmissible spongiform encephalopathies (TSEs)}}
Published	07/28/2024	Amyloid plaques observed in Alzheimers consist mainly of 40-42 amino acid proteins named {{c1::amyloid-beta proteins (ABeta)}}
Published	07/28/2024	Amyloid-beta proteins ia a segment of a 770 amino acid named {{c1::A-beta precursor protein (Beta-PP)}}
Published	07/28/2024	A-beta is excised from beta-PP by proteases called {{c1::beta- and gamma-secretases}}
Published	07/28/2024	In TSEs, the infectious particles is termed a {{c1::prion}}
Published	07/28/2024	The TSE prion consists of aggregated forms of a specific cellular protein, called {{c1::Prpc}} that is normally present in the brian
Published	07/28/2024	What changes in the TSE prion as PrPc is altered and folded into PrPsc
Published	07/28/2024	Why are H bonds and electrostatic forces not very influential in folding of a protein?
Published	07/28/2024	A protein's {{c1::primary structure}} dictates its tertiary structure
Published	07/28/2024	Explain Christian Anfisen's experiment?
Published	07/28/2024	4 steps of protein folding
Published	07/28/2024	What are heat shock chaperones?
Published	07/28/2024	Explain the structure of Beta fibrils?
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