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BIOL 200 UBC Midterm Exam Questions and Answers 100% Pass
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BIOL 200 UBC Midterm Exam Questions and Answers 100% Pass What bonds form in a primary protein structure? - covalent bonds between the backbone, peptide bonds What bonds form in a secondary protein structure? - non covalent bonds between backbone What bonds form in a tertiary protein structur...

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  • 25 de enero de 2025
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  • biol 200 ubc midterm exam questions and answers 10

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BIOL 200 UBC Midterm Exam
Questions and Answers 100% Pass


What bonds form in a primary protein structure? - ✔✔covalent bonds between the

backbone, peptide bonds


What bonds form in a secondary protein structure? - ✔✔non covalent bonds between

backbone


What bonds form in a tertiary protein structure? - ✔✔covalent bonds between R groups

(i.e. disulfide), non-covalent bonds between backbone, R groups


What bonds form in a quaternary protein structure? - ✔✔-covalent bonds between R

groups (i.e. disulfide), non-covalent bonds between backbone, R groups


-between 2+ polypeptides


How is a peptide bond formed? - ✔✔condensation reaction between alpha amino group

of one amino acid and carboxyl group of another


Why are some folding patterns not obtainable by primary structures? - ✔✔resonance

between C-O and C-N constrains flexibility, no free rotation around C-N axis




Katelyn Whitman, All Rights Reserved © 2025 1

, What bonds stabilize primary structures? - ✔✔peptide bonds


What bonds stabilize secondary structures? - ✔✔H-bonds between N-H, C=O groups


What types of structures result from secondary protein folding? - ✔✔alpha helix, beta

sheet


Describe the bonds of an alpha helix. - ✔✔carbonyl forms H-bond with H from N-H of

a residue, 4 residues further on sequence (in same chain), side chains point outward


Describe the bonds of a beta sheet. - ✔✔polypeptide folds back on itself, H-bonds form

between N-H and C=O on neighbouring polypeptide strands, side chains project

upwards & downwards


What factors determine which structure forms in secondary folding? - ✔✔interactions

between side chains of amino acid residues in polypeptide such as: steric hinderance,

charge repulsion, proline presence, presence of other chem groups


What bonds stabilize tertiary structures? - ✔✔ionic bonds between side chains, H-

bonds, LDF (weaker so need more to stabilize), covalent disulfide bond between

cysteine


How does hydrophobic interactions take part in tertiary formation? - ✔✔most stable

when hydrophobic residues face inwards, surrounded by other parts of the protein




Katelyn Whitman, All Rights Reserved © 2025 2

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