leucine rich repeat protein pp32
; protein
; unclassified drug
; urea
; ANP32A protein, human
; signal peptide
; amino terminal sequence
; Article
; carboxy terminal sequence
; controlled study
; hyperbarism
; nuclear magnetic resonance spectroscopy
; priority journal
; protein cavity creation
; protein folding
; protein motif
; protein stability
; protein structure
; protein unfolding
; thermodynamics
; X ray crystallography
; chemistry
; genetics
; human
; mutation
; nuclear magnetic resonance
; protein domain
; protein folding
; small angle scattering
; structure activity relation
; X ray diffraction
; Humans
; Intracellular Signaling Peptides and Proteins
; Mutation
; Nuclear Magnetic Resonance, Biomolecular
; Protein Domains
; Protein Folding
; Protein Stability
; Scattering, Small Angle
; Structure-Activity Relationship
; X-Ray Diffraction
Jenkins, K.A., Graduate Program in Biochemistry and Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Fossat, M.J., Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Department of Biomedical Engineering, Washington University, St. Louis, MO 63130, United States; Zhang, S., Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Rai, D.K., Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853, United States; Klein, S., T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States; Gillilan, R., Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853, United States; White, Z., Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Gerlich, G., Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; McCallum, S.A., Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; Winter, R., Department of Physical Chemistry, Technical University of Dortmund, Dortmund, 44227, Germany; Gruner, S.M., Cornell High Energy Synchrotron Source, Cornell University, Ithaca, NY 14853, United States, Department of Physics, Cornell University, Ithaca, NY 14853, United States, Kavli Institute at Cornell for Nanoscale Science, Cornell University, Ithaca, NY 14853, United States; Barrick, D., T. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States; Royer, C.A., Graduate Program in Biochemistry and Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Department of Biological Sciences, Rensselaer Polytechnic Institute, Troy, NY 12180, United States, Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY 12180, United States
Recommended Citation:
Jenkins K.A.,Fossat M.J.,Zhang S.,et al. The consequences of cavity creation on the folding landscape of a repeat protein depend upon context[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(35)