types of secondary structure and super secondary structure of protein
Leoprabhaleo
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14 slides
May 12, 2023
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About This Presentation
this slides will explain about alpha helix and beta pleated sheets, and types of super secondary structures
Size: 2.32 MB
Language: en
Added: May 12, 2023
Slides: 14 pages
Slide Content
TYPES OF SECONDARY STRUCTURE & SUPER SECONDARY STRUCTURE OF PROTEIN Presented by: LEO PRABHA. A 1 st year MSc Biotechnology Dayananda Sagar University Guided by: Dr. ROSHAN SIR Assistant professor Dayananda Sagar University MSc. Biotechnology 1 st semester/ seminar session 2021
SECONDARY STRUCTURE Local spatial arrangement Dihedral angle, phi and psi Most prominent are α helix and β sheets Stable Consist of : - α - helix - β - pleated sheets - Non repetitive structures - Super secondary structures MSc. Biotechnology 1 st semester/ seminar session 2021 FIG. 6-4 Torsion angles of the polypeptide backbone ( Pg no : 134, Voet & Voet)
ALPHA HELIX Right handed Spiral structure Tightly packed, coiled Side chain extended outwards 3.6 residues per turn, 5.4 A ° pitch Phi- -57 ° & psi- -47 ° Hydrogen bond stabilizing factor, 3H bond per turn Ex α keratin , found in skin, hair and nails MSc. Biotechnology 1 st semester/ seminar session 2021 FIGURE 5–2 Orientation of the main chain atoms of a peptide about the axis of an α helix . Pg no : 103, Harpers illustrated Biochemistry
FIGURE 4–4 Models of the helix, showing different aspects of its structure. (a) Ball-and-stick model showing the intrachain hydrogen bonds. The repeat unit is a single turn of the helix, 3.6 residues. (b) The helix viewed from one end, looking down the longitudinal axis. (c) As this space-filling model shows, the atoms in the center of the helix are in very close contact. ( Pg no : 120, Leininger ) MSc. Biotechnology 1 st semester/ seminar session 2021
α - Keratin α - keratin is coiled coil ( Francis Crick & Linus Pauling ) Right handed helix Strength- mammals, hair, nail & etc intermediate filament(IF) Super twisted coiled coil-5.4 A ° Left handed hydrophobic residues Supramolecular complexes- intermediate filament of hair hardest & toughest α- keratin (Rhinoceros horn) MSc. Biotechnology 1 st semester/ seminar session 2021
BETA SHEETS 2/more polypeptides line up side by side Zig-zag arrangement of chain Β eta strand is extended H bond intra chain 2 residue per turn Stabilized by H bond between carbonyl & amide group R- group protrude from zig-zag in opposite direction Consist of - Parallel - Anti parallel MSc. Biotechnology 1 st semester/ seminar session 2021 FIG. 6-10 Pleated appearance of a 𝛃 sheet (Pg no: 139, Voet & Voet)
BETA SHEETS Parallel : -H bond chain extended in same direction - amino & carbonyl (same) Anti Parallel : -H bond extended in opp direction - amino & carbonyl (opp) Fig: 6.9 beta sheets ( Pg no : 138 Voet & voet) MSc. Biotechnology 1 st semester/ seminar session 2021
SUPER SECONDARY STRUCTURE Folding pattern of secondary structure (Motifs) βαβ motif β hairpin motif α α motif β barrel α β barrel Greek key motif MSc. Biotechnology 1 st semester/ seminar session 2021 FIG. 6-28 Schematic diagrams of super secondary structures. (a) βαβ motif, (b) β hairpin motif, (c) αα motif, and (d) Greek key motif, showing how it is constructed from a folded-over β hairpin. (Pg no: 151 Voet & Voet)
DOMAIN Jane Richardson Large polypeptide Binding of substrate Modular protein Combinations of super secondary elements Small globular protein MSc. Biotechnology 1 st semester/ seminar session 2021
CONCLUSION important roles in protein structure & protein folding used to predict tertiary structure determine the pattern of hydrogen bonding MSc. Biotechnology 1 st semester/ seminar session 2021
REFERENCE Voet & Voet , Fundamental of biochemistry 5 th edition. David L. Nelson & Michael M. Cox ,Principle of biochemistry, 6 th edition David A. Bender & Victor W ,Harpers illustrated biochemistry, 31 st edition MSc. Biotechnology 1 st semester/ seminar session 2021