These authors contributed equally to this work.
Folding of an isolated ribonuclease H core fragment
Version of Record online: 31 DEC 2008
Copyright © 1999 The Protein Society
Volume 8, Issue 11, pages 2251–2257, 1999
How to Cite
Chamberlain, A. K., Fischer, K. F., Reardon, D., Handel, T. M. and Marqusee, S. (1999), Folding of an isolated ribonuclease H core fragment. Protein Science, 8: 2251–2257. doi: 10.1110/ps.8.11.2251
- Issue online: 31 DEC 2008
- Version of Record online: 31 DEC 2008
- Manuscript Accepted: 16 JUL 1999
- Manuscript Received: 15 MAR 1999
- 1995. The thermodynamics of association and unfolding of the 205–316 C-terminal fragment of thermolysin. Biochim Biophys Acta 1252: 95–102. , , , , , .
- 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17: 75–86. , , , .
- 1990. Comparison of different modes of 2-dimensional reverse-correlation NMR for the study of proteins. J Magn Reson 86: 304–318. , , , ,
- 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4: 2455–2468. , ,
- 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28: 7139–7143. , .
- 1969. Conformational studies of a series of overlapping peptides from ribonuclease and their relationship to the protein structure. Biochemistry 8: 2876–2879. , .
- 1996. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat Struct Biol 3: 782–787. , ,
- 1996. IVE (Image Visualization Environment): A software platform for all three-dimensional microscopy applications. J Struct Biol 116: 56–60. , , , , .
- 1996. Presence of a slow dimerization equilibrium on the thermal unfolding of the 205–316 thermolysin fragment at neutral pH. Biochemistry 35: 3477–3486. , .
- 1998. A test of the relationship between sequence and structure in proteins: Excision of the heme binding site in apocytochrome b5. Protein Sci 7: 1983–1993. , , , .
- 1994. Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state. Protein. Sci 3: 1401–1408. ,
- 1996. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry 35: 11951–11958. , ,
- 1994. Folding of apominimyoglobin. Proc Natl Acad Sci USA 91: 11507–11511. , ,
- 1967. Spectroscopie determination of tryptophan and tyrosine in proteins. Biochemistry 6: 1948–1954.
- 1996. Mechanisms and uses of hydrogen exchange. Curr Opin Struct Biol 6: 18–23. , , ,
- 1997. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection. Protein Sci 6: 1885–1892. , , .
- 1997. Importance of the C-terminal helix to the stability and enzymatic activity of Escherichia coli ribonuclease H. Biochemistry 36: 7256–7263. , ,
- 1992a. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114: 6291–6293. ,
- 1992b. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J Magn. Reson. 99: 201–207. ,
- 1992. Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution. J Mol Biol 223: 1029–1052. , , , , , , , ,
- 1989. ANSIG: Program for the assignment of protein 1H 2D NMR spectra by interactive computer graphics. J Magn. Reson. 84: 627–633.
- 1998. Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Sci 7: 96–104. ,
- 1997. NMR structure of the 35-residue villin headpiece subdomain. Nat Struct Biol 4: 180–184. , , .
- 1988. A peptide model of a protein folding intermediate. Nature 336: 42–48. ,
- 1994. A protein dissection study of a molten globule. Biochemistry 33: 2136–2141. , .
- 1997. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nat Struct Biol 4: 298–304. ,
- 1994. NMR solution structure of the C-terminal fragment 255–316 of thermolysin: A dimer formed by subunits having the native structure. Biochemistry 33: 14834–14847. , , , ,
- 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27: 8063–8068. , .
- 1997. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. In: RichardsFM, EisenbergDS, KimPS, eds. Advances in protein chemistry. San Diego: Academic Press. pp 61–122. , ,
- 1990. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor. Nature 344: 685–688. , .
- 1969. An experimental approach to the study of the folding of staphylococcal nuclease. J Biol Chem 244: 3864–3875. , .
- 1992. Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor. Science 255: 594–597. ,
- 1995. NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation. Proteins 22: 41–44. ,
- 1994. The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4: 171–180. , .
- 1994. Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. Biochemistry 33: 7345–7353. , , .