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Protein Structure and Function Insights: A Detailed Overview

This comprehensive guide explores the intricacies of protein structure, covering topics such as secondary and tertiary structures, motifs, supersecondary structures, quaternary arrangement, active sites, and crystallographic interactions. Learn about helices, sheets, turns, motifs, Ramachandran diagrams, and more in this rich resource on protein science.

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Protein Structure and Function Insights: A Detailed Overview

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  1. C to C Phi φ N to N Psi ψ Takes 4 atoms to define rotation about a bond! Trans vs. Cis peptide bonds Trans, carbonyl oxygen is on opposite side of peptide bond from amide hydrogen Fischer & Sumner Proteins have regular structure Hydrophobic effect Helices (, 310, π) n to n+4, n to n+3, n to n+5  has 3.6 residues/turn, 1.5Å rise/residue -sheets parallel, antiparallel, mixed 3.5Å (C - C) Turns Must connect secondary structure somehow – usually not regular structure so backbone exposed

  2. Sequence preference for helices, sheets, turns(loops) Helices usually are amphipathic, so are sheets! Where do the sidechains point? Motifs H-L-H, -H-, -hairpin, Greek key Ramachandran diagrams – 3 major regions (B, A, L) Staggaered conformation of sidechains (rotomers) Supersecondary structure Domains, mosaic proteins Tertiary, Quaternary structure  structures,  structures, / structures,  +  structures

  3. Where might you guess is the active site??

  4. A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange Kent L. Rossman,1 David K. Worthylake,2 Jason T. Snyder, 1 David P. Siderovski,2,3 Sharon L. Campbell,1,3 and John Sondek1,2,3,4

  5. Nature Reviews Molecular Cell Biology6, 167-180 (2005);

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