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216 related items for PubMed ID: 25227444
21. Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone. Stites WE, Pranata J. Proteins; 1995 Jun; 22(2):132-40. PubMed ID: 7567961 [Abstract] [Full Text] [Related]
22. Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids. Dames SA, Aregger R, Vajpai N, Bernado P, Blackledge M, Grzesiek S. J Am Chem Soc; 2006 Oct 18; 128(41):13508-14. PubMed ID: 17031964 [Abstract] [Full Text] [Related]
24. Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants. Schweitzer-Stenner R. J Phys Chem B; 2009 Mar 05; 113(9):2922-32. PubMed ID: 19243204 [Abstract] [Full Text] [Related]
27. Helix propensities calculations for amino acids in alanine based peptides using Jarzynski's equality. Echeverria I, Amzel LM. Proteins; 2010 Apr 05; 78(5):1302-10. PubMed ID: 20014024 [Abstract] [Full Text] [Related]
28. Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. Thompson PA, Eaton WA, Hofrichter J. Biochemistry; 1997 Jul 29; 36(30):9200-10. PubMed ID: 9230053 [Abstract] [Full Text] [Related]
31. Length dependence of the coil <--> beta-sheet transition in a membrane environment. Meier M, Seelig J. J Am Chem Soc; 2008 Jan 23; 130(3):1017-24. PubMed ID: 18163629 [Abstract] [Full Text] [Related]
32. Crystal-state conformation of Calpha,alpha-dialkylated peptides containing chiral beta-homo-residues. Romanelli A, Garella I, Menchise V, Iacovino R, Saviano M, Montesarchio D, Didierjean C, Di Lello P, Rossi F, Benedetti E. J Pept Sci; 2001 Jan 23; 7(1):15-26. PubMed ID: 11245201 [Abstract] [Full Text] [Related]
34. Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains. Schweitzer-Stenner R, Hagarman A, Toal S, Mathieu D, Schwalbe H. Proteins; 2013 Jun 23; 81(6):955-67. PubMed ID: 23229832 [Abstract] [Full Text] [Related]
37. A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems. Chen CC, Zhu Y, King JA, Evans LB. Biopolymers; 1992 Oct 23; 32(10):1375-92. PubMed ID: 1420965 [Abstract] [Full Text] [Related]
38. Protein design simulations suggest that side-chain conformational entropy is not a strong determinant of amino acid environmental preferences. Hu X, Kuhlman B. Proteins; 2006 Mar 15; 62(3):739-48. PubMed ID: 16317667 [Abstract] [Full Text] [Related]
39. Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study. Meral D, Toal S, Schweitzer-Stenner R, Urbanc B. J Phys Chem B; 2015 Oct 22; 119(42):13237-51. PubMed ID: 26418575 [Abstract] [Full Text] [Related]
40. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Lee KH, Xie D, Freire E, Amzel LM. Proteins; 1994 Sep 22; 20(1):68-84. PubMed ID: 7824524 [Abstract] [Full Text] [Related] Page: [Previous] [Next] [New Search]