Single-shot NMR measurement of protein unfolding landscapes

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1824, Issue 6, 2012, Pages 842-849

  Rennella, Enrico ^a   Corazza, Alessandra ^a,d   Codutti, Luca ^a   Causero, Araldo ^b   Bellotti, Vittorio ^c,d   Stoppini, Monica ^c,d   Viglino, Paolo ^a,d   Fogolari, Federico ^a,d   Esposito, Gennaro ^a,d  

^a UNIVERSITY OF UDINE   (Italy)

^b SANTA MARIA DELLA MISERICORDIA UNIVERSITY HOSPITAL   (Italy)

^c UNIVERSITY OF PAVIA   (Italy)

^d NATIONAL INSTITUTE OF BIOSTRUCTURES AND BIOSYSTEMS   (Italy)

Author keywords

Energy landscape; H D exchange; Protein NMR; Protein thermal denaturation; Protein unfolding; Unfolding thermodynamics

Indexed keywords

AMYLOID; BETA 2 MICROGLOBULIN; BUFFER; LIGAND; PROTEIN; UBIQUITIN;

ANALYTIC METHOD; AQUEOUS SOLUTION; ARTICLE; ATOM; BLUU TRAMP; CONTROLLED STUDY; EQUILIBRIUM CONSTANT; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; HUMAN; JOINT; MACROMOLECULE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN UNFOLDING; PROTEOMICS; PROTON NUCLEAR MAGNETIC RESONANCE; SYNOVIAL FLUID; TEMPERATURE MEASUREMENT; THERMODYNAMICS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BAYES THEOREM; BETA 2-MICROGLOBULIN; BUFFERS; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; SYNOVIAL FLUID; THERMODYNAMICS; UBIQUITIN;

EID: 84860361268     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.04.002     Document Type: Article

References (18)

1. Y. Bai, T.R. Sosnick, L. Mayne, and S.W. Englander Protein folding intermediates: native-state hydrogen exchange Science 269 1995 192 197
2. T. Sivaraman, C.B. Arrington, and A.D. Robertson Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin Nat. Struct. Biol. 8 2001 331 333 (Pubitemid 32275018)
3. S.W. Englander, and N.R. Kallenbach Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16 1983 521 655
4. J. Floege, and G. Ehlerding Beta-2-microglobulin-associated amyloidosis Nephron 72 1996 9 26 (Pubitemid 26009466)
5. Y. Bai, J.S. Milne, L. Mayne, and S.W. Englander Primary structure effects on peptide group hydrogen exchange Proteins 17 1993 75 86 (Pubitemid 23261059)
6. J.L. Marmorino, D.S. Auld, S.F. Betz, D.F. Doyle, G.B. Young, and G.J. Pielak Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c Protein Sci. 2 1993 1966 1974 (Pubitemid 23328551)
7. A. Hvidt, and S.O. Nielsen Hydrogen exchange in proteins Adv. Protein Chem. 21 1966 287 386
8. H. Xiao, J.K. Hoerner, S.J. Eyles, A. Dobo, E. Voigtman, A.I. Mel'čuk, and I.A. Kaltashov Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment Protein Sci. 14 2005 543 557 (Pubitemid 40194607)
9. G. Schwarz Estimating the dimension of a model Ann. Stat. 6 1978 461 464
10. P. Schanda, E. Kupce, and B. Brutscher SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds J. Biomol. NMR 33 2005 199 211 (Pubitemid 43118574)
11. F. Delaglio, S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer, and A. Bax NMRPipe - a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
12. C.G. Benitez-Cardoza, K. Stott, M. Hirshberg, H.M. Went, D.N. Woolfson, and S.E. Jackson Exploring sequence/folding space: folding studies on multiple hydrophobic core mutants of ubiquitin Biochemistry 43 2004 5195 5203 (Pubitemid 38620911)
13. H.S. Chung, and A. Tokmakoff Temperature-dependent downhill unfolding of ubiquitin. II. Modeling the free energy surface Proteins 72 2008 488 497 (Pubitemid 351809182)
14. E. Rennella, A. Corazza, F. Fogolari, P. Viglino, S. Giorgetti, M. Stoppini, V. Bellotti, and C. Esposito Equilibrium unfolding thermodynamics of beta2-microglobulin analyzed through native-state H/D exchange Biophys. J. 96 2009 169 179
15. M. Sakata, E. Chatani, A. Kameda, K. Sakurai, H. Naiki, and Y. Goto Kinetic coupling of folding and prolyl isomerization of β2-microglobulin studied by mutational analysis J. Mol. Biol. 382 2008 1242 1255
16. D. Canet, A.M. Last, P. Tito, M. Sunde, A.M. Spencer, D.B. Archer, C. Redfield, C.V. Robinson, and C.M. Dobson Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme Nat. Struct. Biol. 9 2002 308 315 (Pubitemid 34289905)
17. P. Schanda, V. Forge, and B. Brutscher Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy Proc. Natl. Acad. Sci. U. S. A. 104 2007 11257 11262 (Pubitemid 47175128)
18. S.J. Hagen, J. Hofrichter, A. Szabo, and W.A. Eaton Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding Proc. Natl. Acad. Sci. U. S. A. 93 1996 11615 11617 (Pubitemid 26347170)