FOR THE RECORD
The role of protein stability, solubility, and net charge in amyloid fibril formation
Version of Record online: 1 JAN 2009
Copyright © 2003 The Protein Society
Volume 12, Issue 10, pages 2374–2378, October 2003
How to Cite
Schmittschmitt, J. P. and Scholtz, J. M. (2003), The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Science, 12: 2374–2378. doi: 10.1110/ps.03152903
- Issue online: 1 JAN 2009
- Version of Record online: 1 JAN 2009
- Manuscript Accepted: 7 JUL 2003
- Manuscript Revised: 3 JUL 2003
- Manuscript Received: 21 APR 2003
- 1998. Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 31: 297–355.
- 1999. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. 96: 3590–3594. , , , , , , and
- 2000. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19: 1441–1449. , , , , , and
- 1967a. Amyloidosis. N. Engl. J. Med. 277: 522–530.
- 1967b. Amyloidosis (concluded). N. Engl. J. Med. 277: 628–638.
- 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24: 329–332.
- 2001. The structural basis of protein folding and its links with human disease. Philos. Trans. R. Soc. Lond. B 356: 133–145.
- 2001. Amyloid fibrils from muscle myoglobin. Nature 410: 165–166. , , and
- 1980a. Amyloid deposits and amyloidosis. The β-fibrilloses (first of two parts). N. Engl. J. Med. 302: 1283–1292.
- 1980b. Amyloid deposits and amyloidosis: The β-fibrilloses (second of two parts). N. Engl. J. Med. 302: 1333–1343.
- 1997. Purification of ribonucleases Sa, Sa2, and Sa3 after expression in Escherichia coli. Protein Expr. Purif. 11: 162–168. , , , , , , , , and
- 2002. Dependence of α-synuclein aggregate morphology on solution conditions. J. Mol. Biol. 322: 383–393. , , , , , and
- 2001. An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured. Biochemistry 40: 11442–11452. , , , , , , and
- 2001. Prediction of amyloid fibril-forming proteins. J. Biol. Chem. 276: 12945–12950. , , , , and
- 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6: 11–17.
- 2001a. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40: 3525–3535. , , , , , , and
- 2001b. Is Congo red an amyloid-specific dye? J. Biol. Chem. 276: 22715–22721. , , , and
- 2000. Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain. J. Mol. Biol. 300: 541–549. , , , , , , , and
- 1996. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry 35: 6470–6482. , , and
- 1998. Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module. J. Mol. Biol. 280: 245–258. , , , , , and
- 1997. Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol:water mixtures back to water. Biochemistry 36: 8413–8421. and
- 2001. Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism. Biochemistry 40: 6036–6046. , , , , , , , and
- 1990. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29: 2564–2572. , , and
- 1998. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3. J. Mol. Biol. 279: 271–286. , , , , , , , , , , et al.
- 1993. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362: 553–557. , , , , , , , , , , et al.
- 1976. Thermodynamic investigations of proteins. I. Standard functions for proteins with lysozyme as an example. Biophys. Chem. 4: 23–32. and
- 2000. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc. Natl. Acad. Sci. 97: 8979–8984. , , and
- 1997. Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state. Methods Enzymol. 276: 23–59. and
- 2000. Amyloid fibrillogenesis: Themes and variations. Curr. Opin. Struct. Biol. 10: 60–68. and
- 1990. Solubility as a function of protein structure and solvent components. Biotechnology 8: 308–317.
- 2001. The effect of net charge on the solubility, activity, and stability of ribonuclease Sa. Protein Sci. 10: 1206–1215. , , , , and
- 2002. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J. Biol. Chem. 277: 12657–12665. , , , , , and
- 2001. Folding and aggregation are selectively influenced by the conformational preferences of the α-helices of muscle acylphosphatase. J. Biol. Chem. 276: 37149–37154. , , , , , and
- 2002. Ideas of order for amyloid fibril structure. Structure 10: 1031–1036.
- 1996. Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Ab. J. Mol. Biol. 256: 870–877. , , , and