abs

학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 08월 18일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제108회 대한화학회 학술발표회, 총회 및 기기전시회 안내 The Stability of α-helix Conformation of the Different-located Lysine Residue in Alanine-based Model Peptide Complexes with 18-Crown-6 Ether

등록일
2011년 8월 1일 15시 09분 26초
접수번호
1195
발표코드
PHYS.O-7 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 16시 : 20분
발표형식
구두발표
발표분야
물리화학 - Recent Trends in Physical Chemistry
저자 및
공동저자
고재윤, 허성우, 김형준1, 김준곤
포항공과대학교 화학과, Korea
1KAIST EEWS대학원, Korea
The α-helical property of polyalanine-based peptides in gas phase are studied with different-located of a lysine residue in protein and formed non-covalent complex through host-guest interaction between lysine residue and 18-crown-6 ether (18C6). We have investigated the structure of acetylated alanine-based model peptide series, Ac-Ala9-n-LysH+-Alan (n = 0, 1, 3, 5, 7, and 9), and their non-covalent complexes with 18C6 in gas phase using travelling wave ion mobility mass spectrometry (TWIM-MS) and molecular dynamic (MD) simulation. When the lysine residue locates nearby C-terminus, burylammonium group of lysine interacts with carbonyl group of C-terminus. This phenomenon induces the helical structure. On the other hand, when butylammonium group of lysine residue is protected by 18C6, methylene group of 18C6 interacts with carbonyl group of C-terminus and the α-helical properties are enhanced in complex of acetylated alanine-based model peptide with 18C6.

상단으로