The pH-dependent tertiary structure of a designed helix–loop–helix dimer
- 1 October 1997
- journal article
- Published by Elsevier in Folding and Design
- Vol. 2 (5) , 319-330
- https://doi.org/10.1016/s1359-0278(97)00043-6
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Structure and Function of an Aromatic Ensemble That Restricts the Dynamics of the Hydrophobic Core of a Designed Helix-Loop-Helix DimerJournal of the American Chemical Society, 1997
- Use of Aromatic Amino Acid Residues To Restrict the Dynamics in the Hydrophobic Core of a Designed Helix−Loop−Helix DimerJournal of the American Chemical Society, 1996
- Design of a Monomeric 23-Residue Polypeptide with Defined Tertiary StructureScience, 1996
- Toward the Synthesis of a Photosynthetic Reaction Center Maquette: A Cofacial Porphyrin Pair Assembled between Two Subunits of a Synthetic Four-Helix Bundle Multiheme ProteinJournal of the American Chemical Society, 1996
- Controlling Topology and Native-like Behavior of de Novo-Designed Peptides: Design and Characterization of Antiparallel Four-Stranded Coiled CoilsBiochemistry, 1996
- Protein Design: A Hierarchic ApproachScience, 1995
- A de Novo Designed Protein Mimics the Native State of Natural ProteinsJournal of the American Chemical Society, 1995
- Synthesis, structure and activity of artificial, rationally designed catalytic polypeptidesNature, 1993
- Metal Ion-Dependent Modulation of the Dynamics of a Designed ProteinScience, 1993
- Synthesis and biophysical characterization of engineered topographic immunogenic determinants with .alpha..alpha. topologyBiochemistry, 1990