Labhardt AM - Search Results

1

Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements.

Labhardt AM. Labhardt AM. J Mol Biol. 1982 May 15;157(2):357-71. doi: 10.1016/0022-2836(82)90239-x. J Mol Biol. 1982. PMID: 6286980 No abstract available.

2

Secondary structure in ribonuclease. I. Equilibrium folding transitions seen by amide circular dichroism.

Labhardt AM. Labhardt AM. J Mol Biol. 1982 May 15;157(2):331-55. doi: 10.1016/0022-2836(82)90238-8. J Mol Biol. 1982. PMID: 6286979 No abstract available.

3

Recombination of S-peptide with S-protein during folding of ribonuclease S. I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein.

Labhardt AM, Baldwin RL. Labhardt AM, et al. J Mol Biol. 1979 Nov 25;135(1):231-44. doi: 10.1016/0022-2836(79)90349-8. J Mol Biol. 1979. PMID: 43398 No abstract available.

4

Recombination of S-peptide with S-protein during folding of ribonuclease S. II. Kinetic characterization of a stable folding intermediate shown by S-protein at pH 1.7.

Labhardt AM, Baldwin RL. Labhardt AM, et al. J Mol Biol. 1979 Nov 25;135(1):245-54. doi: 10.1016/0022-2836(79)90350-4. J Mol Biol. 1979. PMID: 43399 No abstract available.

5

Nature of the fast and slow refolding reactions of iron(III) cytochrome c.

Ridge JA, Baldwin RL, Labhardt AM. Ridge JA, et al. Among authors: labhardt am. Biochemistry. 1981 Mar 17;20(6):1622-30. doi: 10.1021/bi00509a033. Biochemistry. 1981. PMID: 6261802

6

Measurement of the refolding combination reaction between S-peptide and S-protein.

Labhardt AM, Ridge JA, Lindquist RN, Baldwin RL. Labhardt AM, et al. Biochemistry. 1983 Jan 18;22(2):321-7. doi: 10.1021/bi00271a014. Biochemistry. 1983. PMID: 6402007

7

Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A.

Kiefhaber T, Labhardt AM, Baldwin RL. Kiefhaber T, et al. Among authors: labhardt am. Nature. 1995 Jun 8;375(6531):513-5. doi: 10.1038/375513a0. Nature. 1995. PMID: 7777063

8

Folding intermediates studied by circular dichroism.

Labhardt AM. Labhardt AM. Methods Enzymol. 1986;131:126-35. doi: 10.1016/0076-6879(86)31038-3. Methods Enzymol. 1986. PMID: 3773754 No abstract available.

9

The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.

Klaus W, Gsell B, Labhardt AM, Wipf B, Senn H. Klaus W, et al. Among authors: labhardt am. J Mol Biol. 1997 Dec 12;274(4):661-75. doi: 10.1006/jmbi.1997.1396. J Mol Biol. 1997. PMID: 9417943

10

Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly.

Labhardt AM. Labhardt AM. Proc Natl Acad Sci U S A. 1984 Dec;81(24):7674-8. doi: 10.1073/pnas.81.24.7674. Proc Natl Acad Sci U S A. 1984. PMID: 6595655 Free PMC article.

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