








|
5) Secondary structure of Protein 5.1 Alpha helixccccRefer to Pt-2 sect-6 Connect peptide bond portions to each other as shown in Fig-3. Without turning HN-CO bond portion, insert the ends of oxygen at C=O successively into the hydrogen bond portion (this is attached to 4th nitrogen), while turning the bond portion of alpha carbon little by little to a (normally counter-clockwise) spiraling direction. Then, the Alpha helix is formed as shown is the Fig-4. |
![]() ![]() Fig. 4 |
|
5.2 Parallel Beta-sheet Place 2 peptide bond portions (Bio-101), already connected in a standard form, to same direction (from N-ends to CO-ends). Parallel Beta-sheet is formed when the hydrogen bond portions of one peptide chain (called A) are connected with those of the other (called B) as shown in the Fig-5. Parallel Beta-sheet takes a form of large waves and the side chain will point up and doun. |
![]() ![]() Fig. 5 |
|
5.3 Anti Parallel Beta-sheet Prepare 2 standard formed peptide chains. Place 1 peptide chain to a direction from N-ends to CO-ends, and the other one to reverse direction. The Anti Parallel Beta-sheet is formed when N of 1 peptide (A) and CO of the other are connected together using hydrogen bond parts. Anti Parallel Beta-sheet takes a form of waves and side chain points up and down, same as the parallel one. |
![]() ![]() Fig. 6 |
|
HGS Molecular Structure Model HGS HINOMOTO PLASTICS CO., LTD. 1-10-24, Meguro-Honcho, Meguro-ku, Tokyo, Japan PHONE: +81-3-3714-7226 FAX: +81-3-3714-4657 E-MAIL(technical support): hgs@po.sphere.ne.jp E-MAIL(order support): t_kaneko@maruzen.co.jp |