Lebedenko O, Salikov V, Izmailov S, Podkorytov I, Skrynnikov N
Biophys J. 2023; 123(1):80-100.
PMID: 37990496
PMC: 10808029.
DOI: 10.1016/j.bpj.2023.11.020.
Gupta M, Uversky V
Int J Mol Sci. 2023; 24(3).
PMID: 36768742
PMC: 9916686.
DOI: 10.3390/ijms24032424.
Singh R, Hassan M, Islam A, Ahmad F
PLoS One. 2015; 10(6):e0128740.
PMID: 26046628
PMC: 4457810.
DOI: 10.1371/journal.pone.0128740.
Sargeant D, Gryk M, Maciejewski M, Thapar V, Kundeti V, Rajasekaran S
PLoS One. 2012; 7(12):e49957.
PMID: 23236358
PMC: 3517595.
DOI: 10.1371/journal.pone.0049957.
Bradley J, OMeara F, Farrell D, Nielsen J
Biophys J. 2012; 102(7):1636-45.
PMID: 22500764
PMC: 3318136.
DOI: 10.1016/j.bpj.2012.02.048.
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy V, Kaufman G, Urbach A, Gitlin I, Gudiksen K, Weibel D
Chem Rev. 2008; 108(3):946-1051.
PMID: 18335973
PMC: 2740730.
DOI: 10.1021/cr050262p.
Characterizing residual structure in disordered protein States using nuclear magnetic resonance.
Eliezer D
Methods Mol Biol. 2006; 350:49-67.
PMID: 16957317
PMC: 8604418.
DOI: 10.1385/1-59745-189-4:49.
Reassessing random-coil statistics in unfolded proteins.
Fitzkee N, Rose G
Proc Natl Acad Sci U S A. 2004; 101(34):12497-502.
PMID: 15314216
PMC: 514656.
DOI: 10.1073/pnas.0404236101.
Protein stability in mixed solvents: a balance of contact interaction and excluded volume.
Schellman J
Biophys J. 2003; 85(1):108-25.
PMID: 12829469
PMC: 1303070.
DOI: 10.1016/S0006-3495(03)74459-2.
Polyproline II structure in a sequence of seven alanine residues.
Shi Z, Olson C, Rose G, Baldwin R, Kallenbach N
Proc Natl Acad Sci U S A. 2002; 99(14):9190-5.
PMID: 12091708
PMC: 123116.
DOI: 10.1073/pnas.112193999.
A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins.
Sinha A, Yadav S, Ahmad R, Ahmad F
Biochem J. 2000; 345 Pt 3:711-7.
PMID: 10642532
PMC: 1220808.
Thermal denaturation of iso-1-cytochrome c variants: comparison with solvent denaturation.
Herrmann L, Bowler B
Protein Sci. 1997; 6(3):657-65.
PMID: 9070448
PMC: 2143682.
DOI: 10.1002/pro.5560060315.
The problem of the stability globular proteins.
Pfeil W
Mol Cell Biochem. 1981; 40(1):3-28.
PMID: 7031463
DOI: 10.1007/BF00230185.
The sequential unfolding of ribonuclease A: detection of a fast initial phase in the kinetics of unfolding.
Tsong T, Baldwin R, Elson E
Proc Natl Acad Sci U S A. 1971; 68(11):2712-5.
PMID: 5288248
PMC: 389507.
DOI: 10.1073/pnas.68.11.2712.
Methacarn (methanol-Carnoy) fixation. Practical and theoretical considerations.
PUCHTLER H, Waldrop F, Meloan S, Terry M, Conner H
Histochemie. 1970; 21(2):97-116.
PMID: 4907154
DOI: 10.1007/BF00306176.
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.
Garel J, Baldwin R
Proc Natl Acad Sci U S A. 1973; 70(12):3347-51.
PMID: 4519627
PMC: 427234.
DOI: 10.1073/pnas.70.12.3347.
Acid-induced folding of proteins.
Goto Y, Calciano L, Fink A
Proc Natl Acad Sci U S A. 1990; 87(2):573-7.
PMID: 2153957
PMC: 53307.
DOI: 10.1073/pnas.87.2.573.
Biophysical analysis of phaseolin denaturation induced by urea, guanidinium chloride, pH, and temperature.
Dyer J, Nelson J, Murai N
J Protein Chem. 1992; 11(3):281-8.
PMID: 1388671
DOI: 10.1007/BF01024867.
Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species.
Garel J, Nall B, Baldwin R
Proc Natl Acad Sci U S A. 1976; 73(6):1853-7.
PMID: 1064858
PMC: 430405.
DOI: 10.1073/pnas.73.6.1853.
