Osterhout JJ - Search Results

1

Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol.

Knubovets T, Osterhout JJ, Connolly PJ, Klibanov AM. Knubovets T, et al. Among authors: osterhout jj. Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1262-7. doi: 10.1073/pnas.96.4.1262. Proc Natl Acad Sci U S A. 1999. PMID: 9990012 Free PMC article.

2

Solution structure of alpha t alpha, a helical hairpin peptide of de novo design.

Fezoui Y, Connolly PJ, Osterhout JJ. Fezoui Y, et al. Among authors: osterhout jj. Protein Sci. 1997 Sep;6(9):1869-77. doi: 10.1002/pro.5560060907. Protein Sci. 1997. PMID: 9300486 Free PMC article.

3

Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies.

Knubovets T, Osterhout JJ, Klibanov AM. Knubovets T, et al. Among authors: osterhout jj. Biotechnol Bioeng. 1999 Apr 20;63(2):242-8. Biotechnol Bioeng. 1999. PMID: 10099601

4

Fundamental processes of protein folding: measuring the energetic balance between helix formation and hydrophobic interactions.

Xian W, Connolly PJ, Oslin M, Hausrath AC, Osterhout JJ. Xian W, et al. Among authors: osterhout jj. Protein Sci. 2006 Sep;15(9):2062-70. doi: 10.1110/ps.062297006. Epub 2006 Aug 1. Protein Sci. 2006. PMID: 16882995 Free PMC article.

5

De novo design and structural characterization of an alpha-helical hairpin peptide: a model system for the study of protein folding intermediates.

Fezoui Y, Weaver DL, Osterhout JJ. Fezoui Y, et al. Among authors: osterhout jj. Proc Natl Acad Sci U S A. 1994 Apr 26;91(9):3675-9. doi: 10.1073/pnas.91.9.3675. Proc Natl Acad Sci U S A. 1994. PMID: 8170968 Free PMC article.

6

Dissection of the de novo designed peptide alpha t alpha: stability and properties of the intact molecule and its constituent helices.

Fezoui Y, Braswell EH, Xian W, Osterhout JJ. Fezoui Y, et al. Among authors: osterhout jj. Biochemistry. 1999 Mar 2;38(9):2796-804. doi: 10.1021/bi9823838. Biochemistry. 1999. PMID: 10052951

7

Strategies and rationales for the de novo design of a helical hairpin peptide.

Fezoui Y, Weaver DL, Osterhout JJ. Fezoui Y, et al. Among authors: osterhout jj. Protein Sci. 1995 Feb;4(2):286-95. doi: 10.1002/pro.5560040215. Protein Sci. 1995. PMID: 7757017 Free PMC article.

8

Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores.

Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI. Choe SE, et al. Biochemistry. 1998 Oct 13;37(41):14508-18. doi: 10.1021/bi980889k. Biochemistry. 1998. PMID: 9772179

9

Understanding protein folding through peptide models.

Osterhout JJ. Osterhout JJ. Protein Pept Lett. 2005 Feb;12(2):159-64. doi: 10.2174/0929866053005890. Protein Pept Lett. 2005. PMID: 15723642 Review.

10

A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils.

Fezoui Y, Hartley DM, Walsh DM, Selkoe DJ, Osterhout JJ, Teplow DB. Fezoui Y, et al. Among authors: osterhout jj. Nat Struct Biol. 2000 Dec;7(12):1095-9. doi: 10.1038/81937. Nat Struct Biol. 2000. PMID: 11101888 Free article.

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