TY - JOUR
T1 - De novo design, expression, and characterization of Felix
T2 - A four-helix bundle protein of native-like sequence
AU - Hecht, Michael H.
AU - Richardson, Jane S.
AU - Richardson, David C.
AU - Ogden, Richard C.
PY - 1990
Y1 - 1990
N2 - The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly α-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.
AB - The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly α-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure.
UR - http://www.scopus.com/inward/record.url?scp=0025040232&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025040232&partnerID=8YFLogxK
U2 - 10.1126/science.2392678
DO - 10.1126/science.2392678
M3 - Review article
C2 - 2392678
AN - SCOPUS:0025040232
VL - 249
SP - 884
EP - 891
JO - Science
JF - Science
SN - 0036-8075
IS - 4971
ER -