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Items: 1 to 50 of 92

1.

One sequence plus one mutation equals two folds.

Shortle D.

Proc Natl Acad Sci U S A. 2009 Dec 15;106(50):21011-2. doi: 10.1073/pnas.0912370107. Epub 2009 Dec 8. No abstract available.

2.

Conformational preference of polyglycine in solution to elongated structure.

Ohnishi S, Kamikubo H, Onitsuka M, Kataoka M, Shortle D.

J Am Chem Soc. 2006 Dec 20;128(50):16338-44.

PMID:
17165789
3.

Characterization of denatured proteins using residual dipolar couplings.

Gebel EB, Shortle D.

Methods Mol Biol. 2007;350:39-48.

PMID:
16957316
4.

Multiple alignment tensors from a denatured protein.

Gebel EB, Ruan K, Tolman JR, Shortle D.

J Am Chem Soc. 2006 Jul 26;128(29):9310-1.

PMID:
16848448
5.
7.
8.

Direct demonstration of structural similarity between native and denatured eglin C.

Ohnishi S, Lee AL, Edgell MH, Shortle D.

Biochemistry. 2004 Apr 13;43(14):4064-70.

PMID:
15065848
9.
11.

Propensities, probabilities, and the Boltzmann hypothesis.

Shortle D.

Protein Sci. 2003 Jun;12(6):1298-302.

12.

Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.

Choy WY, Shortle D, Kay LE.

J Am Chem Soc. 2003 Feb 19;125(7):1748-58.

PMID:
12580600
13.

Observation of residual dipolar couplings in short peptides.

Ohnishi S, Shortle D.

Proteins. 2003 Mar 1;50(4):546-51.

PMID:
12577260
14.
15.

The expanded denatured state: an ensemble of conformations trapped in a locally encoded topological space.

Shortle D.

Adv Protein Chem. 2002;62:1-23. Review. No abstract available.

PMID:
12418099
18.

Persistence of native-like topology in a denatured protein in 8 M urea.

Shortle D, Ackerman MS.

Science. 2001 Jul 20;293(5529):487-9.

19.

Prediction of protein structure.

Shortle D.

Curr Biol. 2000 Jan 27;10(2):R49-51. No abstract available.

21.
23.

Structure prediction: The state of the art.

Shortle D.

Curr Biol. 1999 Mar 25;9(6):R205-9.

24.

Protein folding as seen from water's perspective.

Shortle D.

Nat Struct Biol. 1999 Mar;6(3):203-5. No abstract available.

PMID:
10074933
25.

Clustering of low-energy conformations near the native structures of small proteins.

Shortle D, Simons KT, Baker D.

Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11158-62.

30.
35.

Protein folding for realists: a timeless phenomenon.

Shortle D, Wang Y, Gillespie JR, Wrabl JO.

Protein Sci. 1996 Jun;5(6):991-1000. Review.

36.

Contributions of the ionizable amino acids to the stability of staphylococcal nuclease.

Meeker AK, Garcia-Moreno B, Shortle D.

Biochemistry. 1996 May 21;35(20):6443-9.

PMID:
8639591
37.

Structural analysis of non-native states of proteins by NMR methods.

Shortle DR.

Curr Opin Struct Biol. 1996 Feb;6(1):24-30. Review.

PMID:
8696969
38.
40.

The emerging role of insertions and deletions in protein engineering.

Shortle D, Sondek J.

Curr Opin Biotechnol. 1995 Aug;6(4):387-93. Review.

PMID:
7579648
41.

NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.

Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D.

J Mol Biol. 1995 Jul 7;250(2):134-43.

PMID:
7608966
42.

Initial studies of the equilibrium folding pathway of staphylococcal nuclease.

Wang Y, Alexandrescu AT, Shortle D.

Philos Trans R Soc Lond B Biol Sci. 1995 Apr 29;348(1323):27-34.

PMID:
7770483
43.

Protein fold recognition.

Shortle D.

Nat Struct Biol. 1995 Feb;2(2):91-3. No abstract available.

PMID:
7749925
44.

Staphylococcal nuclease: a showcase of m-value effects.

Shortle D.

Adv Protein Chem. 1995;46:217-47. Review. No abstract available.

PMID:
7771319
45.

Electrophoretic characterization of the denatured states of staphylococcal nuclease.

Creighton TE, Shortle D.

J Mol Biol. 1994 Oct 7;242(5):670-82.

PMID:
7932723
46.

Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease.

Alexandrescu AT, Shortle D.

J Mol Biol. 1994 Sep 30;242(4):527-46.

PMID:
7932708
47.

Assignment of amino acid type in 1H-15N correlation spectra by labeling with 14N-amino acids.

Shortle D.

J Magn Reson B. 1994 Sep;105(1):88-90. No abstract available.

PMID:
7921674
48.

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.

Alexandrescu AT, Abeygunawardana C, Shortle D.

Biochemistry. 1994 Feb 8;33(5):1063-72.

PMID:
8110737
49.

Evidence for strained interactions between side-chains and the polypeptide backbone.

Stites WE, Meeker AK, Shortle D.

J Mol Biol. 1994 Jan 7;235(1):27-32.

PMID:
8289248
50.

Alpha helix propensity of amino acids.

Shortle D, Clarke N.

Science. 1993 Nov 5;262(5135):917-8. No abstract available.

PMID:
8235616

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