Gupta M, Uversky V
Int J Mol Sci. 2023; 24(3).
PMID: 36768742
PMC: 9916686.
DOI: 10.3390/ijms24032424.
Wakayama K, Kimura S, Kobatake Y, Kamishina H, Nishii N, Takashima S
Molecules. 2023; 28(1).
PMID: 36615350
PMC: 9822309.
DOI: 10.3390/molecules28010156.
Bychkova V, Dolgikh D, Balobanov V, Finkelstein A
Molecules. 2022; 27(14).
PMID: 35889244
PMC: 9319461.
DOI: 10.3390/molecules27144361.
Uversky V, Finkelstein A
Biomolecules. 2019; 9(12).
PMID: 31817975
PMC: 6995567.
DOI: 10.3390/biom9120842.
Wang C, Aleksandrov A, Yang Z, Forouhar F, Proctor E, Kota P
J Biol Chem. 2018; 293(46):17685-17704.
PMID: 29903914
PMC: 6240863.
DOI: 10.1074/jbc.RA117.000819.
Structure-function relationships in human testis-determining factor SRY: an aromatic buttress underlies the specific DNA-bending surface of a high mobility group (HMG) box.
Racca J, Chen Y, Maloy J, Wickramasinghe N, Phillips N, Weiss M
J Biol Chem. 2014; 289(47):32410-29.
PMID: 25258310
PMC: 4239596.
DOI: 10.1074/jbc.M114.597526.
Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.
Kjaergaard M, Poulsen F, Teilum K
Biophys J. 2012; 102(7):1627-35.
PMID: 22500763
PMC: 3318130.
DOI: 10.1016/j.bpj.2012.02.014.
The molten globule state is unusually deformable under mechanical force.
Elms P, Chodera J, Bustamante C, Marqusee S
Proc Natl Acad Sci U S A. 2012; 109(10):3796-801.
PMID: 22355138
PMC: 3309780.
DOI: 10.1073/pnas.1115519109.
Conformational folding and stability of the HET-C2 glycolipid transfer protein fold: does a molten globule-like state regulate activity?.
Kenoth R, Kamlekar R, Simanshu D, Gao Y, Malinina L, Prendergast F
Biochemistry. 2011; 50(23):5163-71.
PMID: 21553912
PMC: 3134308.
DOI: 10.1021/bi200382c.
Translational and rotational motions of albumin sensed by a non-covalent associated porphyrin under physiological and acidic conditions: a fluorescence correlation spectroscopy and time resolved anisotropy study.
Andrade S, Costa S, Borst J, van Hoek A, Visser A
J Fluoresc. 2008; 18(3-4):601-10.
PMID: 18264814
DOI: 10.1007/s10895-008-0329-y.
Characterization of protein-folding pathways by reduced-space modeling.
Kmiecik S, Kolinski A
Proc Natl Acad Sci U S A. 2007; 104(30):12330-5.
PMID: 17636132
PMC: 1941469.
DOI: 10.1073/pnas.0702265104.
Biophysical characterization of Z(SPA-1)--a phage-display selected binder to protein A.
Lendel C, Dincbas-Renqvist V, Flores A, Wahlberg E, Dogan J, Nygren P
Protein Sci. 2004; 13(8):2078-88.
PMID: 15238637
PMC: 2279809.
DOI: 10.1110/ps.04728604.
Protein stability induced by ligand binding correlates with changes in protein flexibility.
Celej M, Montich G, Fidelio G
Protein Sci. 2003; 12(7):1496-506.
PMID: 12824495
PMC: 2323922.
DOI: 10.1110/ps.0240003.
An affibody in complex with a target protein: structure and coupled folding.
Wahlberg E, Lendel C, Helgstrand M, Allard P, Dincbas-Renqvist V, Hedqvist A
Proc Natl Acad Sci U S A. 2003; 100(6):3185-90.
PMID: 12594333
PMC: 152267.
DOI: 10.1073/pnas.0436086100.
Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysis.
Polverino de Laureto P, Frare E, Gottardo R, Van Dael H, Fontana A
Protein Sci. 2002; 11(12):2932-46.
PMID: 12441391
PMC: 2373748.
DOI: 10.1110/ps.0205802.
Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments.
Chakshusmathi G, Ratnaparkhi G, Madhu P, Varadarajan R
Proc Natl Acad Sci U S A. 1999; 96(14):7899-904.
PMID: 10393919
PMC: 22159.
DOI: 10.1073/pnas.96.14.7899.
Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state.
Rankin S, Watts A, Roder H, Pinheiro T
Protein Sci. 1999; 8(2):381-93.
PMID: 10048331
PMC: 2144269.
DOI: 10.1110/ps.8.2.381.
Folding pathway of a lattice model for proteins.
Pande V, Rokhsar D
Proc Natl Acad Sci U S A. 1999; 96(4):1273-8.
PMID: 9990014
PMC: 15453.
DOI: 10.1073/pnas.96.4.1273.
Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.
Kim S, Baum J
Protein Sci. 1998; 7(9):1930-8.
PMID: 9761473
PMC: 2144173.
DOI: 10.1002/pro.5560070908.
Probing minimal independent folding units in dihydrofolate reductase by molecular dissection.
Gegg C, Bowers K, Matthews C
Protein Sci. 1997; 6(9):1885-92.
PMID: 9300488
PMC: 2143800.
DOI: 10.1002/pro.5560060909.