?url_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rft.relation=http%3A%2F%2Fd-scholarship-dev.library.pitt.edu%2F9507%2F&rft.title=SPECTROSCOPIC+INVESTIGATION+OF+PROTEINS&rft.creator=Kabagambe%2C+Benjamin&rft.description=Apomyoglobin+is+obtained+from+pure+myoglobin+by+extracting+out+the+heme+group.+UsingUV-visible+spectrometry+we+are+able+to+monitor+complete+removal+of+heme+group.+Thisextraction+initiates+the+disruption+of+myoglobin's+tertiary+conformation.+Apomyoglobin+consistsof+8+%CE%B1-helices+labeled+A+through+H.+These+helices+unfold+when+the+protein+is+subjected+to+pHdecrease.+It+is+more+compact+at+about+pH+7+and+unfolds+as+we+change+to+more+acidicenvironment.+At+about+pH+2+we+have+A%2C+G%2C+H+core+with+the+rest+of+the+helices+unfolded.+At+pHvalues+slightly+lower+than+2%2C+A%2C+G+and+H+helices+are+also+unfolded.+When+the+protein+is+notdenatured%2C+the+refolding+process+is+done+by+changing+the+pH+towards+neutral.+At+pH+2%2C+G+and+Hhelices+refold+and+at+pH+4+A-helix+refolds+as+well.+We+have+been+able+to+label+A-helix+withprotons+and+the+rest+of+the+protein+with+deuterium+using+H2O+and+D2O+respectively.+We+havethen+used+temperature+change+to+initiate+the+unfolding+of+protonated+A-helix.+When+dissolved+inD2O%2C+the+protonated+A-helix+at+elevated+temperatures%2C+exchanges+its+N-H+protons+to+N-Ddeuterons.+Temperatures+were+elevated+from+0+%C2%B0C+to+80+%C2%B0C+and+changes+in+Am+III+peak+intensitieswere+observed+using+UV+resonance+Raman+spectroscopy.+These+peak+changes+were+quantifiedand+used+to+calculate+the+number+of+N-H+bonds+present+between+0+%C2%B0C+and+80+%C2%B0C.+The+number+ofN-H+bonds+decreased+with+increase+in+temperature+indicating+the+unfolding+of+A-helix.&rft.date=2008-01-17&rft.type=University+of+Pittsburgh+ETD&rft.type=PeerReviewed&rft.format=application%2Fpdf&rft.language=en&rft.identifier=http%3A%2F%2Fd-scholarship-dev.library.pitt.edu%2F9507%2F1%2FKabagambebenjamin_etdPitt2007.pdf&rft.identifier=++Kabagambe%2C+Benjamin++(2008)+SPECTROSCOPIC+INVESTIGATION+OF+PROTEINS.++Master's+Thesis%2C+University+of+Pittsburgh.++++(Unpublished)++