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1984 4
1987 4
1989 4
1990 2
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1992 1
1993 3
1994 1
1996 1
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1998 1
1999 2
2000 4
2001 2
2002 3
2003 3
2004 3
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106 results

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Page 1
Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment.
Sukumar M, Gierasch LM. Sukumar M, et al. Fold Des. 1997;2(4):211-22. doi: 10.1016/S1359-0278(97)00030-8. Fold Des. 1997. PMID: 9269562
BACKGROUND: As an approach to understanding the role of local sequence in determining protein tertiary structure, we have examined the conformation of a 23-residue peptide fragment corresponding to the structurally conserved helix-Schellman motif-helix (H-Sm-H …
BACKGROUND: As an approach to understanding the role of local sequence in determining protein tertiary structure, we have examined the confo …
Protein stability curves.
Becktel WJ, Schellman JA. Becktel WJ, et al. Biopolymers. 1987 Nov;26(11):1859-77. doi: 10.1002/bip.360261104. Biopolymers. 1987. PMID: 3689874 No abstract available.
The thermodynamic stability of proteins.
Schellman JA. Schellman JA. Annu Rev Biophys Biophys Chem. 1987;16:115-37. doi: 10.1146/annurev.bb.16.060187.000555. Annu Rev Biophys Biophys Chem. 1987. PMID: 3297085 Review. No abstract available.
Diabetes mellitus due to misfolding of a beta-cell transcription factor: stereospecific frustration of a Schellman motif in HNF-1alpha.
Narayana N, Phillips NB, Hua QX, Jia W, Weiss MA. Narayana N, et al. J Mol Biol. 2006 Sep 22;362(3):414-29. doi: 10.1016/j.jmb.2006.06.086. Epub 2006 Jul 27. J Mol Biol. 2006. PMID: 16930618
Diabetes-associated mutation G20R perturbs the dimerization domain of HNF-1alpha, an intertwined four-helix bundle. In the wild-type structure G20 participates in a Schellman motif to cap an alpha-helix; its dihedral angles lie in the right side of the Ramachandran plot (a …
Diabetes-associated mutation G20R perturbs the dimerization domain of HNF-1alpha, an intertwined four-helix bundle. In the wild-type structu …
A C-H triplebond O hydrogen bond stabilized polypeptide chain reversal motif at the C terminus of helices in proteins.
Madan Babu M, Kumar Singh S, Balaram P. Madan Babu M, et al. J Mol Biol. 2002 Sep 27;322(4):871-80. doi: 10.1016/s0022-2836(02)00715-5. J Mol Biol. 2002. PMID: 12270720
From a dataset of 634 proteins, 1304 helices terminating in a Schellman motif have been examined. The C-H triplebond O interaction between the T-4 C(alpha)H and T+1 Cz doublebond O group (C triplebond O< or =3.5A) becomes possible only when the T+1 residue …
From a dataset of 634 proteins, 1304 helices terminating in a Schellman motif have been examined. The C-H triplebond O interac …
An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix.
Aravinda S, Shamala N, Pramanik A, Das C, Balaram P. Aravinda S, et al. Biochem Biophys Res Commun. 2000 Jul 14;273(3):933-6. doi: 10.1006/bbrc.2000.3026. Biochem Biophys Res Commun. 2000. PMID: 10891350
The extended conformation at (D)Leu(9) results in a compact folded structure, stabilized by a potentially strong C-H. O hydrogen bond between Ala(4) C(alpha)H and (D)Leu(9) CO. The parameters for C-H. O interaction are Ala(4) C(alpha)H. O=C (D)Leu(9) d …
The extended conformation at (D)Leu(9) results in a compact folded structure, stabilized by a potentially strong C-H. O hydrogen bond …
Simultaneous Measurement of Muon Neutrino nu_{mu} Charged-Current Single pi^{+} Production in CH, C, H_{2}O, Fe, and Pb Targets in MINERvA.
Bercellie A, Kroma-Wiley KA, Akhter S, Ahmad Dar Z, Akbar F, Ansari V, Ascencio MV, Athar MS, Bellantoni L, Betancourt M, Bodek A, Bonilla JL, Bravar A, Budd H, Caceres G, Cai T, Díaz GA, da Motta H, Dytman SA, Felix J, Fields L, Filkins A, Fine R, Gago AM, Gallagher H, Gaur PK, Ghosh A, Gilligan SM, Gran R, Granados E, Harris DA, Jena D, Jena S, Kleykamp J, Klustová A, Kordosky M, Last D, Le T, Lozano A, Lu XG, Mahbub I, Maher E, Manly S, Mann WA, Mauger C, McFarland KS, Messerly B, Miller J, Moreno O, Morfín JG, Naples D, Nelson JK, Nguyen C, Olivier A, Paolone V, Perdue GN, Plows KJ, Ramírez MA, Ransome RD, Ray H, Ruterbories D, Schellman H, Solano Salinas CJ, Su H, Sultana M, Syrotenko VS, Utt B, Valencia E, Vaughan NH, Waldron AV, Yaeggy B, Zazueta L; MINERvA Collaboration. Bercellie A, et al. Phys Rev Lett. 2023 Jul 7;131(1):011801. doi: 10.1103/PhysRevLett.131.011801. Phys Rev Lett. 2023. PMID: 37478458
Simultaneous Measurement of nu_{mu} Quasielasticlike Cross Sections on CH, C, H_{2}O, Fe, and Pb as a Function of Muon Kinematics at MINERvA.
Kleykamp J, Akhter S, Ahmad Dar Z, Ansari V, Ascencio MV, Sajjad Athar M, Bashyal A, Bercellie A, Betancourt M, Bodek A, Bonilla JL, Bravar A, Budd H, Caceres G, Cai T, Carneiro MF, Díaz GA, da Motta H, Dytman SA, Felix J, Fields L, Filkins A, Fine R, Gago AM, Gallagher H, Gilligan SM, Gran R, Granados E, Harris DA, Henry S, Jena D, Jena S, Klustová A, Kordosky M, Last D, Lozano A, Lu XG, Maher E, Manly S, Mann WA, Mauger C, McFarland KS, Messerly B, Miller J, Moreno O, Morfín JG, Naples D, Nelson JK, Nguyen C, Olivier A, Paolone V, Perdue GN, Plows KJ, Ramírez MA, Ransome RD, Ray H, Ruterbories D, Schellman H, Solano Salinas CJ, Su H, Sultana M, Syrotenko VS, Valencia E, Vaughan NH, Waldron AV, Wret C, Yaeggy B, Zazueta L; MINERvA Collaboration. Kleykamp J, et al. Phys Rev Lett. 2023 Apr 21;130(16):161801. doi: 10.1103/PhysRevLett.130.161801. Phys Rev Lett. 2023. PMID: 37154647
The thermodynamics of solvent exchange.
Schellman JA. Schellman JA. Biopolymers. 1994 Aug;34(8):1015-26. doi: 10.1002/bip.360340805. Biopolymers. 1994. PMID: 8075384
A model for solvation in mixed solvents, which was developed for the free energy and preferential interaction [J. A. Schellman (1987), Biopolymers, Vol. 26, pp. 549-559; (1990), Biophysical Chemistry, Vol. 37, pp. 121-140; (1993), Biophysical Chemistry, Vol. 45, pp. 273-27 …
A model for solvation in mixed solvents, which was developed for the free energy and preferential interaction [J. A. Schellman (1987) …
Kaj Ulrik Linderstrøm-Lang (1896-1959).
Schellman JA, Schellman CG. Schellman JA, et al. Protein Sci. 1997 May;6(5):1092-100. doi: 10.1002/pro.5560060516. Protein Sci. 1997. PMID: 9144781 Free PMC article.
After the war, a number of major advances were being made that would revolutionize the field of protein chemistry (Pauling and Corey's H-bonded structures, Sanger's sequencing techniques, chromatography, Watson and Crick structures, modern instrumentation). ...
After the war, a number of major advances were being made that would revolutionize the field of protein chemistry (Pauling and Corey's H …
106 results