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Conformation of the backbone in unfolded proteins.
Department of Chemistry, New York University, 100 Washington Place, New York, New York 10003-5180, USA.
PMID: 16683759 [PubMed - indexed for MEDLINE]
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Cited by 9 PubMed Central articles
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The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.
Beck DA, Alonso DO, Inoyama D, Daggett V.
Proc Natl Acad Sci U S A. 2008 Aug 26; 105(34):12259-64. Epub 2008 Aug 19.
[Proc Natl Acad Sci U S A. 2008]
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Are current molecular dynamics force fields too helical?
Best RB, Buchete NV, Hummer G.
Biophys J. 2008 Jul; 95(1):L07-9. Epub 2008 May 2.
[Biophys J. 2008]
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Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain.
Wells M, Tidow H, Rutherford TJ, Markwick P, Jensen MR, Mylonas E, Svergun DI, Blackledge M, Fersht AR.
Proc Natl Acad Sci U S A. 2008 Apr 15; 105(15):5762-7. Epub 2008 Apr 7.
[Proc Natl Acad Sci U S A. 2008]
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