article
; binding affinity
; biological activity
; consensus sequence
; high temperature
; low temperature
; protein family
; protein function
; protein stability
; consensus sequence
; genetics
; temperature
; thermodynamics
; protein
; Consensus Sequence
; Proteins
; Temperature
; Thermodynamics
Sternke, M., T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States; Tripp, K.W., T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States; Barrick, D., T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, United States
Recommended Citation:
Sternke M.,Tripp K.W.,Barrick D.. Consensus sequence design as a general strategy to create hyperstable; biologically active proteins[J]. Proceedings of the National Academy of Sciences of the United States of America,2019-01-01,166(23)