Structural Diversity in Protein Physics and Secondary Structures: Chirality, Helices, and Bonds

Nov 26, 2025

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Explore the intricate world of protein physics lecture 7, delving into main and secondary structures, H-bonds, and mirror-asymmetric amino acids. This lecture covers topics like right and left mirror-asymmetric helices, α-helices, 310 helix, β-sheets, collagen triple helix, and experimental studies using X-ray crystallography, NMR spectroscopy, Far UV CD spectra, and IR spectra to analyze secondary structures. Discover the role of hydrogen bonds and hydrophobic interactions in membrane, globular, and fibrous proteins.

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Structural Diversity in Protein Physics and Secondary Structures: Chirality, Helices, and Bonds

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PROTEIN PHYSICS LECTURE 7
Main secondary structures
H-bonds Helices: Right and Left
Mirror-asymmetric amino acids – mirror-asymmetric (“chiral”) helices Right -helix
Right -helix
Right -helix Right 310 helix

ALA, etc. GLY only

, twisted
, twisted
Mirror-asymmetric amino acids – mirror-asymmetric twist of -sheets
-hairpin with turn
turn I turn I’ turn II
-bulge
collagen triple helix
Experimental study of secondary structure X-ray crystallography NMR spectroscopy (cross-peaks)
Experimental study of secondary structure Far UV CD spectra (peptide groups) IR spectra (amid I, C=O bond)