Notes in BIOL 3000 Exam 2

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Published	10/06/2023	proteins targeted to mitochondria are {{c1::partially}} folded in the cytosol and must {{c1::unfold and refold}} to enter the matrix
Published	10/06/2023	proteins targeted to the nucleus are {{c1::completely}} folded
Published	10/06/2023	most secreted proteins are initially {{c1::co-translationally}} inserted into the ER lumen
Published	10/06/2023	the number on SRP54 indicates the {{c1::mass in kDA}} of the protein subunit
Published	10/06/2023	the default destination is secretion for proteins that contain {{c1::N-terminal signal sequence}} and {{c1::cotranslationally inserted in the ER}}
Published	10/06/2023	amino acids on SRP54 interact with {{c1::core hydrophobic}} amino acids present on all ER signal sequences
Published	10/06/2023	{{c1::importin}} carries folded proteins to the nucleus
Published	10/06/2023	{{c1::1/3}} of all human proteins enter the secretory pathway
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Published	10/06/2023	N-terminal signal is {{c1::cleaved}} when proteins are contranslationally inserted into the ER
Published	10/06/2023	co-translational insertion into ER requires {{c1::GTP hydrolysis}}
Published	10/06/2023	first {{c1::70}} amino acids of nascent protein must be synthesized for signal sequence to get exposed from ribosome
Published	10/06/2023	SRP54 binds to {{c1::ER signal sequence}}
Published	10/06/2023	SRP9/14 binds to {{c1::ribosome}} and {{c2::arrests translation}}
Published	10/06/2023	SRP68/72 binds to {{c1::the translocon}} and {{c1::transfers ribosome to it}}
Published	10/06/2023	translocon is a {{c1::ribosome gated protein channel}}
Published	10/06/2023	SRP54 and SRP receptor {{c1::hydrolyze GTP}} to dissociate
Published	10/06/2023	signal peptidase removes {{c1::signal sequence}} from {{c1::secretory}} and {{c1::type I integral membrane proteins}}
Published	10/06/2023	SRP54 recognizes ER signal sequences by using {{c1::van der Waal's interactions}} from the amino acids {{c1::MILV}}
Published	10/06/2023	ER signal sequences contain a {{c1::6-12}} sequence {{c1::hydrophobic}} core preceded by at least one {{c1::K or R}}
Published	10/06/2023	what type of protein is this
Published	10/06/2023
Published	10/06/2023	Type II integral membrane proteins do not have {{c1:N-terminal signaling sequences}} and instead have {{c1::internal signal sequences}} that…
Published	10/06/2023	{{c1::disulfide}} bonds form spontaneously in the {{c2::oxidizing}} environment of the ER
Published	10/06/2023	BiP ensures {{c1::hydrophobic}} regions are folded {{c2::within the interior}} of proteins
Published	10/06/2023	N-linked glycosylation {{c1::Man9-Glc1-3}} keep proteins in ER
Published	10/06/2023	converting n-linked glycosylation to {{c1::man8}} allows proteins to leave the ER
Published	10/06/2023	misfolded proteins returned to cytosol through {{c1::dislocon}} which get {{c1::ubiquitinated}} and {{c1::degraded}} by the {{c1::…
Published	10/06/2023	BiP ensures hydrophobic regions are folded into the interior of a protein by {{c1::increasing entropy of surrounding H2O}}
Published	10/06/2023	BiP recognizes stretches of {{c1::7}} amino acids where at least every other amino acid is {{c1::hydrophobic}}
Published	10/06/2023	proteins cannot exit the ER as long as {{c1::BiP}} is bound
Published	10/06/2023	BiP {{c1::pulls}}, {{c1::holds}}, and {{c1::folds}}
Published	10/06/2023	Energy from {{c1::ATP hydrolysis}} when BiP binds also pulls protein into the ER
Published	10/06/2023	Hsps are present in {{c1::cytoplasm}}, {{c1::nucleus}}, and {{c1::mitochondria}} and function similarly to BiP
Published	10/06/2023	BiP ATP is hydrolized by the {{c1::Ire1 Sec63 complex}}
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New Card	10/06/2023	test
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