The coordinates have been deposited in the Brookhaven Protein Data Bank under the file names 1DDS for the wild-type DHFR structure, 1DDR for the structure of DHFR with urea, 1RBX for the wild-type ribonuclease structure, and 1RBW for the structure of ribonuclease with guanidinium.
The effect of denaturants on protein structure†
Version of Record online: 31 DEC 2008
Copyright © 2008 The Protein Society
Volume 6, Issue 8, pages 1727–1733, August 1997
How to Cite
Dunbar, J., Yennawar, H. P., Banerjee, S., Luo, J. and Farber, G. K. (1997), The effect of denaturants on protein structure. Protein Science, 6: 1727–1733. doi: 10.1002/pro.5560060813
- Issue online: 31 DEC 2008
- Version of Record online: 31 DEC 2008
- Manuscript Accepted: 28 APR 1997
- Manuscript Received: 3 MAR 1997
- NIH predoctoral training fellowship
- Office of Naval Research
- National Science Foundation. Grant Number: DMB 9317273
- 1989. Mutational effects on protein stability. Annu Rev Biochem 58: 765–98.
- 1979. Crystallographic studies of the dynamic properties of lysozyme. Nature 280: 563–568. , , , , ,
- 1991. Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths. Proteins Struct Funct Genet 10: 10–21. , , , , , .
- 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J Biol Chem 257: 13650–13662. , , , ,
- 1990. Monte Carlo simulations on the likecharged guanidinium—guanidinium ion pair in water. J Phys Chem 94: 6056–6061. , ,
- 1990. Surface tension measurements show that chaotropic salting-in denaturants are not just water-structure breakers. Proc Natl Acad Sci USA 87: 167–169. ,
- 1987. Crystallographic R factor refinement by molecular dynamics. Science 235: 458–460. , ,
- 1991. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry 30: 2227–2239. ,
- 1990. Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate-NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29: 3263–3277. , ,
- Collaborative Computational Project, Number 4 1994. Acta Cryst D50: 760–763.
- 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis. J Biol Chem 257: 13663–13672. , , ,
- 1976. Low resolution structure of the glycogen phosphorylase A monomer and comparison with phosphorylase B. J Mol Biol 103: 1–13. , , , , .
- 1963. The relationship of structure to the effectiveness of denaturing agents for proteins. Biochemistry 2: 47–57. , .
- 1982. Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K. Proc Natl Acad Sci USA 79: 4967–4971. , , , , ,
- 1991. Calorimetric and volumetric studies of the interactions of some amides in water and in 6 mol dm−3 aqueous guanidinium chloride. J Chem Soc Faraday Trans 87: 2975–2982. , ,
- 1978. Expression of functionality of α–chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation. Biochemistry 17: 5460–5468. ,
- 1992. Model bias in macromolecular crystal structures. Acta Cryst A48: 851–858. , , .
- 1992. Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Eng 5: 791–796. , .
- 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A47: 110–119. , , ,
- 1995. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375: 513–515. , , .
- 1993. Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 32: 9609–9613. ,
- 1956. Crystalline forms of bovine pancreatic ribonuclease: Techniques of preparation, unit cells, and space groups. Acta Crystallogr 9: 460–465. , , ,
- 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283–291. , , , .
- 1985. Study of ethanol-lysozyme interactions using neutron diffraction. Biochemistry 24: 5862–5869. , , .
- 1989. Binding of dimethyl sulfoxide to lysozyme in crystals, studied with neutron diffraction. Biochemistry 28: 7028–7033. ,
- 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study. J Mol Biol 226: 491–505. , .
- 1968. Solvent content of protein crystals. J Mol Biol 33: 491–497. .
- 1967. On the scaling of X-ray photographs. Acta Crystallogr 22: 322. , , .
- 1992. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science 257: 1559–1563. , , ,
- 1984. Fluctuations in protein structure from X-ray diffraction. Annu Rev Biophys Bioeng 13: 331–371. , .
- 1994. A structural basis for the interaction of urea with lysozyme. Protein Sci 3: 706–710. , .
- 1975. Interactions of urea and other polar compounds in water. J Am Chem Soc 97: 631–640. , .
- 1987. The thermodynamic stability of proteins. Ann Rev Biophys Biophys Chem 16: 115–137. .
- 1953. The kinetics of protein denaturation. I. The behavior of the optical rotation of ovalbumin in urea solutions. J Am Chem Soc 75: 5139–5152. ,
- 1974. Crystallographic study of the interaction of urea with lysozyme. Nature 250: 295–298. , , , .
- 1993. Peptide-urea interactions as observed in diketopiperazine-urea cocrystal. Biophys Chem 46: 165–169. , , , , .
- 1992. Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320 K. Biochemistry 31: 2469–2481. , , .
- 1992. Water as ligand: Preferential hydration and exclusion of denaturants in protein unfolding. Biochemistry 31: 9857–9864. .
- 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu Rev Biophys Biomol Struct 22: 67–97. .
- 1964. Nonpolar group participation in the denaturation of proteins by urea and guanidinium salts. Model compound studies. J Am Chem Soc 86: 508–514. , , , .
- 1949. The probability distribution of X-ray intensities. Acta Crystallogr 2: 318–321.
- 1983. Structure of ribonuclease A: Results of joint neutron and X-ray refinement at 2.0 Å resolution. Biochemistry 22: 2720–2728. ,
- 1995. A structural explanation for enzyme memory in nonaqueous solvents. J Am Chem Soc 117: 577–585. , , .
- 1994. The structure of γ–chymotrypsin in hexane. Biochemistry 33: 7326–7336. , , .
- 1977. Crystallographic studies of protein denaturation and renaturation. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme. Biochemistry 16: 1418–1424. , , , ,
- 1978. Structural analysis of denaturant-protein interactions: Comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme. Biophys Struct Mech 4: 27–36. , , , , , ,