Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.

Autor: Loh, S N, Kay, M S, Baldwin, R L

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America; June 1995, Vol. 92 Issue: 12 p5446-5450, 5p

Case study of protein structure, stability, and function: NMR investigations of the proline residues in staphylococcal nuclease

Autor: Markley, J. L., Hinck, A. P., Loh, S. N., Prehoda, K., Truckses, D., Walkenhorst, W. F., Wang, J.

Publikováno v: Pure & Applied Chemistry; January 1994, Vol. 66 Issue: 1 p65-69, 5p

On the nature of conformational openings: native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin.

Autor: Feng Z; Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 E. Adams Street, Syracuse, NY 13210, USA., Butler MC, Alam SL, Loh SN

Publikováno v: Journal of molecular biology [J Mol Biol] 2001 Nov 16; Vol. 314 (1), pp. 153-66.

Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding.

Autor: Feng Z; SUNY Health Science Center at Syracuse, Department of Biochemistry and Molecular Biology, 750 East Adams Street, Syracuse New York 13210, USA., Ha JH, Loh SN

Publikováno v: Biochemistry [Biochemistry] 1999 Nov 02; Vol. 38 (44), pp. 14433-9.

Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: application to staphylococcal nuclease.

Autor: Loh SN; Department of Biochemistry, University of Wisconsin-Madison 53706., Markley JL

Publikováno v: Biochemistry [Biochemistry] 1994 Feb 01; Vol. 33 (4), pp. 1029-36.