Antiparallel pleated beta-sheets observed in crystal structures of N,N- bis(trichloroacetyl) and N,N-bis(m-bromobenzoyl) gramicidin S. Arch Biochem ... K.Ravikumar,B.A.Wallace - Springer Netherlands 被引量: 339发表: 1988年 Stereochemistry of Protected Ornithine Side Chains of Gramicidin S Deriv...
The antiparallel peptide strands are distorted from a regularly pleated sheet, caused mainly by the L-Ala residue in which φ=– 155° and ψ= 162°. In the disulfide bridge C (1)-C β (1)-S(1)-(3′)-C β (3′)-C (3′), S—S = 2.030 , angles C β SS = 107° and ...
versa. The β-sheets are pleated (i.e. they undulate) with the Caatoms alternatively a little above, or a little below the plane of the β-sheet, which means that the side chains project alternatively above and below the plane. β-Strands can interact to form two types of pleated ...
Infrared spectra and resonance interaction of amide‐I vibration of the antiparallel‐chain pleated sheet Theoretical treatment of resonance interaction of amide-I vibration has been done in a dipole-dipole approximation on the basis of perturbation theory. A s... YN Chirgadze,N.A. Nevskaya - ...
Interestingly, the hexamer, 3 shows the first example of antiparallel pleated β‐sheet crystal structure for a depsipeptide molecule. In the packing cells, especially for 3, the ester groups OCO are perpendicularly oriented to the amide groups NHCO and β‐sheet planes to avoid the interaction ...
C. Interestingly, the hexamer, 3 shows the first example of antiparallel pleated -sheet crystal structure for a depsipeptide molecule. In the packing cells, especially for 3 , the ester groups OCO are perpendicularly oriented to the amide groups NHC...
Prediction of strand pairing in antiparallel and parallel beta-sheets using information theory - Steward, Thornton - 2002 () Citation Context ...d pairs.sb) Parallel β-sheet alignment scores: In addition to the side chain position, another aspect is to study the different preferences for ...
The structures are characterized by a dominant family possessing an anti-parallel 尾-pleated sheet that is constrained by the disulphide bridge between Cys4 and Cys13. The two strands of the 尾-sheet are joined by a Type II' 尾-turn spanning the residues Lys7-D-Lys8-Pro9-Tyr10. This ...
The structures are characterized by a dominant family possessing an anti-parallel 尾-pleated sheet that is constrained by the disulphide bridge between Cys4 and Cys13. The two strands of the 尾-sheet are joined by a Type II' 尾-turn spanning the residues Lys7-D-Lys8-Pro9-Tyr10. This ...
Tauro S,Coutinho E,Srivastava S.An antiparallel beta-sheet and a beta-turn characterize the structure of antiviral HⅣ-1 peptide T140, as revealed by 2D NMR and MD Simulations.Protein Peptide Letters. 2003Tauro S;Coutinho E;Srivastava S.An Antiparallel Sheet And Aturn Characterize TheStructure...