tailieunhanh - Lecture Principles of biochemistry - Chapter 4 (part 2): Protein 3-D structure: 3 and 4 structure and protein folding

After studying this chapter you will be able to: Know that primary structure determines protein conformation, define domains, motifs combine through hydrophobic interactions to form domains, know general properties of a protein with 4o structure, know the definition of an oligomeric protein, know 4o structure nomenclature, be able to determine the subunit composition of an oligomeric protein using information obtained from gel permeation chromatography and SDS PAGE analysis,. | Chapter 4: Part 2 Protein 3-D structure: 3o and 4o structure and protein folding. 3o Structure third level of protein organization folding of polypeptide chain causes 2o structures to interact formation of motifs and domains Proteins with similar 1o structure also have similar 3o structure tuna 1 GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKTGQAEGYSYTDANKSKGIVWN yeast 1 GSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVWDE rice 1 GNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTANKMAVIWEE tuna 61 ETLMEYLENPKKYIPGTKMIFAGIKKKGERQDLVAYLKSATS yeast 61 NNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE rice 61 NTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS Common Motifs Motifs Combine to form Domains Hydrophobic interactions are the major driving force in folding domains Alpha/beta barrel Parallel twisted sheet Domains are independent folding units in a 3o structure of a protein Individual domains have specific function lactate dehydrogenase malate dehydrogenase C O O - C H 2 C O C O O - C O O - | Chapter 4: Part 2 Protein 3-D structure: 3o and 4o structure and protein folding. 3o Structure third level of protein organization folding of polypeptide chain causes 2o structures to interact formation of motifs and domains Proteins with similar 1o structure also have similar 3o structure tuna 1 GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKTGQAEGYSYTDANKSKGIVWN yeast 1 GSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIKKNVWDE rice 1 GNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTANKMAVIWEE tuna 61 ETLMEYLENPKKYIPGTKMIFAGIKKKGERQDLVAYLKSATS yeast 61 NNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE rice 61 NTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS Common Motifs Motifs Combine to form Domains Hydrophobic interactions are the major driving force in folding domains Alpha/beta barrel Parallel twisted sheet Domains are independent folding units in a 3o structure of a protein Individual domains have specific function lactate dehydrogenase malate dehydrogenase C O O - C H 2 C O C O O - C O O - C H H O C H 2 C O O - 3 C O O - C H C H H O C O O - C C H 3 O + NADH + NAD+ + NADH + NAD+ Protein family members share common domain structures 4o Structure Quaternary structure describes the organization of subunits in a protein with multiple subunits (oligomeric protein) Can have homo-multimers or hetero-multimers a2b2 a2bg Determine molecular weight of native protein by gel permeation chromatography Determine molecular weight of individual subunits by SDS-PAGE Can use the information to determine subunit composition 4o Structure If . Native protein – 160,000 daltons and a-Subunit – 50,000 daltons b-Subunit – 30,000 daltons Then Protein can have a2b2 structure Subunits held together by non-covalent interactions Oligomeric protein is more stable than disassociated subunits Active site often made up of AA residues from different subunits 4o and 3o structure is often affected by ligand (substrate or inhibitor) binding. Important in enzyme regulation 4o Structure Tm Protein .

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