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BioChem C6:E1
Chapter 6 Exam 1
| Question | Answer |
|---|---|
| Amino acids are linked via a _____ rxn | condensation rxn |
| Amino acids are linked by _____ bonds to form, _______ | peptide, polypeptides |
| electrostatic properties depend primarily on _____ chain | side chains |
| isoelectric point | the pH at which it carries no net charge |
| primary structure | the sequence of amino acid residues |
| secondary structure | the spatial arrangement of the polypeptide backbone, |
| tertiary structure | 3D structure of an entire polypeptide, including all of its side chains |
| Quaternary structure | the spatial arrangement of polypeptide chains in a. protein with multiple subunits |
| secondary structure contd | the polypeptide backbone has limited conformational flexibility, two principal secondary structures, a-helix and B sheets, characterized by hydrogen bonding between the backbone |
| the a helix | hydrogen bonds along the helical axis stabilize this structure, i + 4 patten of H bonds, stabilized by the h bond of the carbonyl group of one amide (I) to the NH of another amide (I +4) |
| the B sheet | antiparallel b sheets align in opposite diections, parallel are in the same direction, h bonding formed between the backbone carbonyl and amino groups, |
| the b sheet | ARE ACROSS THE STRANDS |
| T or F, Proteins can have any combination of secondary structures | True |
| Tertiary structure and protein stability | describes all aspects of the 3D folding in space, a folded polypeptide assumes a shape with a hydrophilic surface and a hydrophobic core (micelle), protien folding and protein stabilization depend on non covalent forces |
| What structure is the hydrophobic effect | tertiary |
| what interactions are tertiary structure stabilized by | non-covalent forces, exception : disulfide between cysteine |
| the most important bond for the a helices and beta sheets are | h bonds |
| cys residues can form _____ bonds | disulfide |
| Quaternary structure contd | Proteins containing more than one polypeptide chain have quaternary structure , two or more separate chains (subunits) can orients in 3D space to give structure |
| T or F, when mis folded proteins are not immediately refolded/degraded but instead aggregate as insoluble fibers, patients will be totally cool | False, no it leads to disease duh ex Alzheimers |
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