Alkyl Isocyanides Serve as Transition State Analogues for Ligand Entry and Exit in Myoglobin
Author:
Affiliation:
1. Department of Biochemistry and Cell Biology and W. M. Keck Center for Computational Biology, Rice University, Houston, Texas 77005
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi1001745
Reference38 articles.
1. Straight-Chain Alkyl Isocyanides Open the Distal Histidine Gate in Crystal Structures of Myoglobin,
2. The Stretching Frequencies of Bound Alkyl Isocyanides Indicate Two Distinct Ligand Orientations within the Distal Pocket of Myoglobin
3. Ligand Migration in Sperm Whale Myoglobin
4. Mapping the Pathways for O2 Entry Into and Exit from Myoglobin
5. Ligand pathways in myoglobin: A review of trp cavity mutations
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