Alternative packing arrangements in the hydrophobic core of lambda repressor.
The random alteration of hydrophobic core positions in the N-terminal domain of lambda-repressor, both individually and in combination, shows that there are many ways of repacking the core of the protein. Although the number of functional sequences is limited by constraints on composition, volume and steric interactions, the simple requirement that these positions remain hydrophobic is the main determinant of whether a core sequence is compatible with the wild-type fold.
Lim
W A
WA
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Sauer
R T
RT
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000235:genetics; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004268:DNA-Binding Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D012097:Repressor Proteins / Q000235:genetics; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000235:genetics; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins