1986 Fiscal Year Final Research Report Summary
Stability of Protein Secondary Structures: Study with Synthetic Peptides as a Model.
| Project/Area Number |
60580220
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
生物物性学
|
|---|
| Research Institution | Kyoto University |
|---|
Principal Investigator |
TAKAHASHI Sho Institute for Chemical Research, Kyoto University, 化学研究所, 助教授 (20022593)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
OOI Tatsuo Institute for Chemical Research, Kyoto University, 化学研究所, 教授 (00027012)
|
|---|
| Project Period (FY) |
1985 – 1986
|
| Keywords | Protein secondary structure / Block copolypeptide / <alpha> -helix / <beta> -structure / Circular dichroism / Solid-phase peptide synthesis |
|---|
| Research Abstract |
1. Effect of electric charge in the neighbor of <alpha> -helix. Two kinds of block copolypeptides, <(Lys)_(20)> <(Ala)_(20)> Phe ( <I> ) and <(Ala)_(20)> <(Lys)_(20)> Phe ( <II> ), were synthesized by dipeptide coupling employing a solid-phase methodolog and compared for their <alpha> -helical contents under various vonditions. Results clearly showed that the peptide <II> was always more <alpha> -helical when the amino groups of lysyl side chains dissociated, namely, <alpha> -helix is more stable when positive charges are located in the environment next to the C-terminal of the helix. Coupled to our previous study, the interaction between an <alpha> -helix dipole and external charges is quite large and cannot be neglected in a prediction of <alpha> -helix.
2. A variety of hexapeptides, Cys-X-A-B-Y-Cus, was synthesized in an attempt to evaluate parameters related to <beta> -structure propensity, and a possibility in obtaining such parameters by determination of a redox equilibrium was checked. The results proved such an approach was very promising.
|
