N. Zhou

发表

Relationship of sidechain hydrophobicity and α‐helical propensity on the stability of the single‐stranded amphipathic α‐helix

R. Hodges, C. Kay, T. J. Sereda, 1995 .

Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic .alpha.-helical peptides

R. Hodges, B. Sykes, N. Zhou, 1992 .

Comparison of antiparallel and parallel two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization.

R. Hodges, C. Kay, O. Monera, 1993, The Journal of biological chemistry.

The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability.

R. Hodges, C. Kay, N. Zhou, 1994, Protein engineering.

Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: amphipathic alpha-helices.

C. Mant, R. Hodges, N. Zhou, 1990, Peptide research.

Comparison of silica-based cyanopropyl and octyl reversed-phase packings for the separation of peptides and proteins.

C. Mant, R. Hodges, N. Zhou, 1991, Journal of chromatography.

Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils.

R. Hodges, C. Kay, N. Zhou, 1992, The Journal of biological chemistry.

Synthetic model proteins: contribution of hydrophobic residues and disulfide bonds to protein stability.

R. Hodges, C. Kay, P. Semchuk, 1990, Peptide research.

The role of interchain ionic interactions in protein folding and stability of two-stranded α-helical coiled-coils

R. Hodges, C. Kay, N. Zhou, 1994 .

Importance of intra-chain ionic interactions in stabilizing α-helices in proteins

R. Hodges, C. Kay, N. Zhou, 1993 .

The two‐stranded α‐helical coiled‐coil is an ideal model for studying protein stability and subunit interactions

R. Hodges, C. Kay, N. Zhou, 1992, Biopolymers.

Chapter 13 Amino acids and peptides

C. Mant, R. Hodges, N. Zhou, 1992 .

Disulfide bond contribution to protein stability: positional effects of substitution in the hydrophobic core of the two-stranded alpha-helical coiled-coil.

R. Hodges, C. Kay, N. Zhou, 1993, Biochemistry.

Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability.

C. Mant, R. Hodges, N. Zhou, 1994, Journal of chromatography. A.

Relationship of sidechain hydrophobicity and alpha-helical propensity on the stability of the single-stranded amphipathic alpha-helix.

R. Hodges, C. Kay, T. J. Sereda, 1995, Journal of peptide science : an official publication of the European Peptide Society.

A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids.

R. Hodges, B. Sykes, C. Kay, 1993, Biochemistry.

Structure, function and application of the coiled-coil protein folding motif.

R. Hodges, N. Zhou, J. G. Adamson, 1993, Current opinion in biotechnology.

The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils.

R. Hodges, C. Kay, N. Zhou, 1994, Journal of molecular biology.

Design, synthesis and structural characterization of model heterodimeric coiled-coil proteins.

R. Hodges, C. Kay, P. Semchuk, 2009, International journal of peptide and protein research.

Correlation of protein retention times in reversed-phase chromatography with polypeptide chain length and hydrophobicity.

C. Mant, R. Hodges, N. Zhou, 1989, Journal of chromatography.

Formation of Parallel and Antiparallel Coiled-coils Controlled by the Relative Positions of Alanine Residues in the Hydrophobic Core (*)

R. Hodges, C. Kay, P. Lavigne, 1996, The Journal of Biological Chemistry.

Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded alpha-helical coiled-coil.

R. Hodges, C. Kay, N. Zhou, 1992, Biochemistry.