Folding and binding
Current opinion in structural biology
(1996)
6
1
Pathways of protein folding
PROG BIOPHYS MOL BIO
(1996)
65
SA401
Folding & Design: introduction to a new journal
Fold Des
(1996)
1
i
Folding & design: Introduction to a new journal
FOLD DES
(1996)
1
U7
CONFORMATIONAL PATHWAY OF THE POLYPEPTIDE-CHAIN OF CHYMOTRYPSIN INHIBITOR-2 GROWING FROM ITS N-TERMINUS IN-VITRO - PARALLELS WITH THE PROTEIN-FOLDING PATHWAY
Journal of molecular biology
(1995)
254
968
(doi: 10.1006/jmbi.1995.0669)
Perturbed pKA-values in the Denatured States of Proteins
J Mol Biol
(1995)
254
980
(doi: 10.1006/jmbi.1995.0670)
A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding
Journal of molecular biology
(1995)
254
305
(doi: 10.1006/jmbi.1995.0618)
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
J Mol Biol
(1995)
254
260
(doi: 10.1006/jmbi.1995.0616)
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2
Journal of molecular biology
(1995)
254
289
(doi: 10.1006/jmbi.1995.0617)
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.
Proceedings of the National Academy of Sciences
(1995)
92
10869
(doi: 10.1073/pnas.92.24.10869)
Submillisecond events in protein folding.
Proc Natl Acad Sci U S A
(1995)
92
10668
(doi: 10.1073/pnas.92.23.10668)
DISULFIDE MUTANTS OF BARNASE .1. CHANGES IN STABILITY AND STRUCTURE ASSESSED BY BIOPHYSICAL METHODS AND X-RAY CRYSTALLOGRAPHY
Journal of molecular biology
(1995)
253
493
(doi: 10.1006/jmbi.1995.0568)
DISULFIDE MUTANTS OF BARNASE .2. CHANGES IN STRUCTURE AND LOCAL STABILITY IDENTIFIED BY HYDROGEN-EXCHANGE
Journal of molecular biology
(1995)
253
505
(doi: 10.1006/jmbi.1995.0569)
Negative activation enthalpies in the kinetics of protein folding.
Proceedings of the National Academy of Sciences of the United States of America
(1995)
92
8926
(doi: 10.1073/pnas.92.19.8926)
The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.
Proceedings of the National Academy of Sciences
(1995)
92
5326
(doi: 10.1073/pnas.92.12.5326)
Preface
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1995)
348
3
(doi: 10.1098/rstb.1995.0038)
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution
Philosophical Transactions of the Royal Society B Biological Sciences
(1995)
348
11
(doi: 10.1098/rstb.1995.0040)
Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.
Journal of molecular biology
(1995)
248
478
Folding of a nascent polypeptide chain in vitro: Cooperative formation of structure in a protein module
Proc Natl Acad Sci U S A
(1995)
92
3683
(doi: 10.1073/pnas.92.9.3683)
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE BACKBONE C-13, N-15 AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED AND UREA-DENATURED STATES
JOURNAL OF CELLULAR BIOCHEMISTRY
(1995)
42