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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.1
- 수록면
- 497 - 501 (5page)
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초록· 키워드
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Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered 73-residue full transactivation domain (TAD) of the p53 tumor suppressor protein and two peptides: one a wild type p53 TAD peptide with a helix pre-structuring property, and a mutant peptide with a disabled helix-forming propensity. Measurements were carried out in order to characterize their water and ion binding characteristics. By quantifying the number of hydrate water molecules, we provide a microscopic description for the interactions of water with a wild-type p53 TAD and two p53 TAD peptides. The results provide direct evidence that intrinsically disordered proteins (IDPs) and a less structured peptide not only have a higher hydration capacity than globular proteins, but are also able to bind a larger amount of charged solute ions.
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등록된 정보가 없습니다.
참고문헌 (17)
참고문헌 신청
Lee SH / 2012 / Understanding pre-structured motifs(PreSMos)in intrinsically unfolded proteins / Curr Protein Pept Sci 13:34~54
Dunker AK / 2001 / Intrinsically disordered protein / J Mol Graph Model 19:26~59
Uversky VN / 2008 / Intrinsically disordered proteins in human diseases: Introducing the D2 concept / Annu Rev Biophys 37:215~246
Dunker AK / 2000 / Intrinsic protein disorder in complete genomes / Genome Inform 11:161~171
Obradovic Z / 2005 / Exploiting heterogeneous sequence properties improves prediction of protein disorder / PROTEINS:Structure, Function, and Bioinformatics (Suppl 7):176~182
Dunker AK / 2001 / Intrinsically disordered protein / J Mol Graph Model 19:26~59
Uversky VN / 2008 / Intrinsically disordered proteins in human diseases: Introducing the D2 concept / Annu Rev Biophys 37:215~246
Dunker AK / 2000 / Intrinsic protein disorder in complete genomes / Genome Inform 11:161~171
Obradovic Z / 2005 / Exploiting heterogeneous sequence properties improves prediction of protein disorder / PROTEINS:Structure, Function, and Bioinformatics (Suppl 7):176~182
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