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- https://bio.libretexts.org/Courses/Ouachita_Baptist_University/Reyna_Cell_Biology/02%3A_2-(T2-first_lecture)_Protein_Structure/2.03%3A_Understanding_Protein_Conformation/2.3.02%3A_C2._Secondary_StructureSecondary structures are those repetitive structures involving H bond between amide H and carbonyl O in- the main chain. These include alpha helices, beta strands (sheets) and reverse turns.
- https://bio.libretexts.org/Workbench/Biochem_Remix_Acevedo/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.01%3A_Secondary_Structure_and_LoopsA beta sheet would then consist of multiple strands, since each "strand" is separated from other "strands" by an intervening contiguous stretch of amino acid which bends within the protein in a way th...A beta sheet would then consist of multiple strands, since each "strand" is separated from other "strands" by an intervening contiguous stretch of amino acid which bends within the protein in a way that allows the next section of the peptide backbone, the next "strand", to H-bond with the first "strand". But remember, even in this case, all the H-bonds holding the alpha and beta structures together are intramolecular.
- https://bio.libretexts.org/Courses/Wheaton_College_Massachusetts/Principles_of_Biochemistry/04%3A_Protein_structure_and_function/4.03%3A_Secondary_StructureSecondary structures are those repetitive structures involving H bond between amide H and carbonyl O in- the main chain. These include alpha helices, beta strands (sheets) and reverse turns.
- https://bio.libretexts.org/Bookshelves/Biochemistry/Fundamentals_of_Biochemistry_(Jakubowski_and_Flatt)/01%3A_Unit_I-_Structure_and_Catalysis/04%3A_The_Three-Dimensional_Structure_of_Proteins/4.02%3A_Secondary_Structure_and_LoopsThe page provides a detailed exploration of secondary structures in proteins, focusing on alpha helices, beta sheets (parallel and antiparallel), 310 helices, pi helices, and loops and turns. It expla...The page provides a detailed exploration of secondary structures in proteins, focusing on alpha helices, beta sheets (parallel and antiparallel), 310 helices, pi helices, and loops and turns. It explains the roles of hydrogen bonds in stabilizing structures and discusses sequence determinants that influence structural propensities. The text also covers the characteristics and roles of loops, turns, and linkers, and examines amino acid propensities for forming different secondary structures.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.03%3A_Secondary_StructureSecondary structures are those repetitive structures involving H bond between amide H and carbonyl O in- the main chain. These include alpha helices, beta strands (sheets) and reverse turns.
- https://bio.libretexts.org/Courses/Roosevelt_University/BCHM_355_455_Biochemistry_(Roosevelt_University)/04%3A_Proteins-_Structure_and_Folding/4.07%3A_The_Three-Dimensional_Structure_of_Proteins/4.7.02%3A_Secondary_Structure_and_LoopsShifting back to the Greek letter naming system, the gamma turn, the second most common turn, has just three total residues (i th , i th +1, and i th +2) with the hydrogen bond between the backbone ca...Shifting back to the Greek letter naming system, the gamma turn, the second most common turn, has just three total residues (i th , i th +1, and i th +2) with the hydrogen bond between the backbone carbonyl of the i th amino acid and the backbone amide H of the i th +2 amino acid.
