P. A. Kosen

发表

Structure-activity studies of interleukin-2.

F E Cohen, F. Cohen, I. Kuntz, 1986, Science.

Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance.

F E Cohen, E K Bradley, F. Cohen, 1990, Journal of molecular biology.

Spin labeling of proteins.

P. A. Kosen, 1989, Methods in enzymology.

Amide chemical shifts in many helices in peptides and proteins are periodic

I. Kuntz, E. C. Craig, P. A. Kosen, 1991 .

Kinetics of reduction of the intersubunit disulfides of the carboxyl propeptide of type I procollagen.

C. Franzblau, P. A. Kosen, 1982, Biochemistry.

two-dimensional nuclear magnetic resonance

I. Kuntz, P. Kollman, J. Thomason, 1992 .

Two-dimensional 1H NMR of three spin-labeled derivatives of bovine pancreatic trypsin inhibitor.

I. Kuntz, N. Oppenheimer, V. Basus, 1986, Biochemistry.

The structure of the carbohydrate units of the carboxyl-terminal peptide of procollagen as elucidated by 500 MHz 1H-NMR spectroscopy.

G. Gerwig, T. Marti, J. Vliegenthart, 1984, Biochimica et biophysica acta.

Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitor.

E. Blout, T. Creighton, P. A. Kosen, 1980, Biochemistry.

Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor.

E. Blout, T. Creighton, T E Creighton, 1981, Biochemistry.

Disulfide bond-coupled folding of bovine pancreatic trypsin inhibitor derivatives missing one or two disulfide bonds.

I. Kuntz, S. Anderson, A. Falick, 1992, Biochemistry.

Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor

F. Cohen, I. Kuntz, K. Mostov, 1993, The Journal of cell biology.

Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds.

I. Kuntz, S. Anderson, M. Hurle, 1990, Biochemistry.

Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two‐dimensional nuclear magnetic resonance

I. Kuntz, P. Kollman, S. Anderson, 1992, Protein science : a publication of the Protein Society.

Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway.

E. Blout, T. Creighton, P. A. Kosen, 1983, Biochemistry.

Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly

I. Kuntz, S. Anderson, P. A. Kosen, 1987, Science.

Infrared spectroscopy of [2H8]naphthalene in its lowest triplet state

R. Mushlin, P. A. Kosen, R. Clarke, 1973 .

Structural studies of alpha-bungarotoxin. 3. Corrections in the primary sequence and X-ray structure and characterization of an isotoxic alpha-bungarotoxin.

J. Finer-Moore, V. Basus, P. A. Kosen, 1988, Biochemistry.