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Study Guide - Protein Structure

The study guide outlines the four levels of protein structure: primary, secondary, tertiary, and quaternary. It details the characteristics and formation of primary sequences, α-helices, β-pleated sheets, and the overall 3-D conformation of proteins, including interactions that stabilize these structures. Additionally, it explains the significance of structural domains and motifs in protein function.

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11 views2 pages

Study Guide - Protein Structure

The study guide outlines the four levels of protein structure: primary, secondary, tertiary, and quaternary. It details the characteristics and formation of primary sequences, α-helices, β-pleated sheets, and the overall 3-D conformation of proteins, including interactions that stabilize these structures. Additionally, it explains the significance of structural domains and motifs in protein function.

Uploaded by

Zachary Reed
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd

Study Guide: Protein Structure

CHEM 1050
Refer to D2L for weekly objectives and associated readings

Protein structure and function:


Primary Structure:
● Is linear sequence of amino acids in polypeptide chain. Written from the amino terminus (N-terminus) to the carboxyl terminus (C-terminus).

Secondary Structure:
● α-helix: α-helices are formed when the carbonyl group of peptide bond forms a hydrogen bond with the amide nitrogen of another peptide bond four
amino acids down the polypeptide chain.
o The peptide backbone is formed by hydrogen bonds between each carbonyl oxygen atom and the amide hydrogen located 4 residues down the
chain. This unique bonding sequence results in an alpha helix structure that is highly compact and rigid.
o Comprises about a third of all secondary structures.
o Proline is not typically found in these structures as it forms a non-traditional peptide bond and adds a ‘kink’ in the helix.

● β-pleated sheets: β-sheets are formed when β-strands are connected laterally by at least two or three backbone hydrogen bonds.
o The β strands are connected horizontally by hydrogen bonds formed between C=O groups of either strand and NH groups of either strand.
o β pleated sheets can either be parallel or anti-parallel.
o The R groups always protrude to the top or bottom.
o Depending on the R groups on the sides of the β sheet, the sheet may have a hydrophilic and a hydrophobic side. The hydrophilic side of the
sheet will be on the surface of the protein and be exposed to the polar H2O solvent. The hydrophobic side of the sheet will be buried in the
protein and will only rarely be exposed to the polar H2O solvent.

● bends, turns, or loops: Short stretches areas of the polypeptide chain form these structures that are stabilized by hydrogen bonds (these are not
random)

Tertiary Structure (supersecondary structures):


● Tertiary structure is the total 3-D conformation of an entire polypeptide chain including interactions between alpha-helices, beta-sheets and any other
loops, turns, or bends.
o Rossman fold is an example of tertiary structure.
Study Guide: Protein Structure
● Structural domains are defined as a section of protein sufficient to perform a particular chemical or physical task
o These are defined regions with specific function that are conserved in function and sequence across other proteins.
● Motifs are common arrangements of secondary structures to generate a tertiary arrangement

● Tertiary structures can be stabilized by a variety of interactions including: disulfide linkages, hydrophobic interactions, van der Waals forces, electrostatic
interactions and ionic bonding.

Quaternary Structure:
A combination of two or more tertiary subunits that work together as one functioning unit.

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