Structural Diversity in Protein Physics and Secondary Structures: Chirality, Helices, and Bonds
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.
Structural Diversity in Protein Physics and Secondary Structures: Chirality, Helices, and Bonds
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Presentation Transcript
PROTEIN PHYSICS LECTURE 7
H-bonds Helices: Right and Left
Mirror-asymmetric amino acids – mirror-asymmetric (“chiral”) helices Right -helix
Right -helix
Right -helix Right 310 helix
, twisted
, twisted
Mirror-asymmetric amino acids – mirror-asymmetric twist of -sheets
turn I turn I’ turn II
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)
Membrane Globular Fibrous H-bonds & hydrophobics