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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술대회자료
- 저자정보
- 저널정보
- 한국생물정보시스템생물학회 한국생물정보시스템생물학회 심포지엄 한국생물정보시스템생물학회 2000년도 International Symposium on Bioinformatics
- 발행연도
- 2000.1
- 수록면
- 86 - 87 (2page)
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초록· 키워드
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Protein folding is a fundamental problem in structural bioinformatics and so numerous studies have been devoted to the subject. As the most common regular secondary conformation in proteins, helix has been an important ingredient of the protein folding problem. In particular, alanine based polypeptides are widely studied to identify the helix folding process in that the aianine amino acid is known to have one of the highest helix propensities. In principle, intrinsic helix propensities can be obtained from gas-phase measurements where solvent effect is absent. Hudgins et al. studied alanine-based peptides in vacuo using high-resolution ion mobility measurement technique. It was reported that introduction of a single Iysine at the C terminus resulted in the formation of very stable, monomeric polyalanine helices. We also have investigated helix formation in vacuo with different terminal charge conditions; we have found a new type of helix motif, To the best of our knowledge, this type of helix conformation has not been characterized before and we name it as I-helix.
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