Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography.

[1]  A. Forsgren,et al.  “Protein A” from S. Aureus I. Pseudo-Immune Reaction with Human γ-Globulin , 1966 .

[2]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[3]  F. Sanger,et al.  DNA sequencing with chain-terminating inhibitors. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[4]  L. Isaksson,et al.  Analysis of rpsD mutations in Escherichia coli. I. Comparison of mutants with various alterations in ribosomal protein S4. , 1979, Molecular & general genetics : MGG.

[5]  J. Deisenhofer Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution. , 1981, Biochemistry.

[6]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[7]  M. Uhlén,et al.  A synthetic IgG-binding domain based on staphylococcal protein A. , 1987, Protein engineering.

[8]  R. Saiki,et al.  A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. , 1988, Nucleic acids research.

[9]  W C Johnson,et al.  Protein secondary structure and circular dichroism: A practical guide , 1990, Proteins.

[10]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[11]  A. P. Brunet,et al.  The role of turns in the structure of an α-helical protein , 1993, Nature.

[12]  R. L. Baldwin,et al.  Helix capping propensities in peptides parallel those in proteins. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[13]  M. Uhlén,et al.  Engineering proteins to facilitate bioprocessing. , 1994, Trends in biotechnology.

[14]  J. Skolnick,et al.  Monte carlo simulations of protein folding. II. Application to protein A, ROP, and crambin , 1994, Proteins.

[15]  C. Vetriani,et al.  Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare turn mutations that prevent the folding of Rop. , 1994, Journal of molecular biology.

[16]  L Regan,et al.  Redesigning the topology of a four-helix-bundle protein: monomeric Rop. , 1995, Biochemistry.

[17]  M. Uhlén,et al.  A combinatorial library of an α-helical bacterial receptor domain , 1995 .

[18]  Axel T. Brünger,et al.  Amino-acid substitutions in a surface turn modulate protein stability , 1996, Nature Structural Biology.

[19]  G. Montelione,et al.  High-level production of uniformly 15N-and 13C-enriched fusion proteins in Escherichia coli , 1996 .

[20]  A Kolinski,et al.  Folding simulations and computer redesign of protein A three‐helix bundle motifs , 1996, Proteins.

[21]  Mathias Uhlén,et al.  Multiple affinity domains for the detection, purification and immobilization of recombinant proteins , 1996, Journal of molecular recognition : JMR.

[22]  G. Montelione,et al.  The mechanism of binding staphylococcal protein A to immunoglobin G does not involve helix unwinding. , 1996, Biochemistry.

[23]  H. Dyson,et al.  Absence of a stable intermediate on the folding pathway of protein A , 1997, Protein science : a publication of the Protein Society.

[24]  L Regan,et al.  An inverse correlation between loop length and stability in a four-helix-bundle protein. , 1997, Folding & design.

[25]  G T Montelione,et al.  High-resolution solution NMR structure of the Z domain of staphylococcal protein A. , 1997, Journal of molecular biology.

[26]  L. Regan,et al.  Using loop length variants to dissect the folding pathway of a four-helix-bundle protein. , 1999, Journal of molecular biology.