Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 28 September 1990:
Vol. 249. no. 4976, pp. 1544 - 1548
DOI: 10.1126/science.2218495
Prev | Table of Contents | Next

Articles

Science, Vol 249, Issue 4976, 1544-1548
Copyright © 1990 by American Association for the Advancement of Science

articles

Structural characterization of a partly folded apomyoglobin intermediate

FM Hughson, PE Wright, and RL Baldwin

Department of Biochemistry, Beckman Center, Stanford University School of Medicine, CA 94305.

To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize the native state. Proteins in partly folded states can be used to dissect protein organizational hierarchies. A partly folded apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them by two-dimensional 1H-NMR (nuclear magnetic resonance). Protons in the A, G, and H helix regions are protected from exchange, while protons in the B and E helix regions exchange freely. On the basis of these results and the three-dimensional structure of native myoglobin, a structural model is presented for the partly folded intermediate in which a compact subdomain retains structure while the remainder of the protein is essentially unfolded.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.
T. Uzawa, C. Nishimura, S. Akiyama, K. Ishimori, S. Takahashi, H. J. Dyson, and P. E. Wright (2008)
PNAS 105, 13859-13864
   Abstract »    Full Text »    PDF »
Folding Myoglobin within a Sol-Gel Glass: Protein Folding Constrained to a Small Volume.
E. S. Peterson, E. F. Leonard, J. A. Foulke, M. C. Oliff, R. D. Salisbury, and D. Y. Kim (2008)
Biophys. J. 95, 322-332
   Abstract »    Full Text »    PDF »
Protein folding: Independent unrelated pathways or predetermined pathway with optional errors.
S. Bedard, M. M. G. Krishna, L. Mayne, and S. W. Englander (2008)
PNAS 105, 7182-7187
   Abstract »    Full Text »    PDF »
Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution.
R. Horst, W. A. Fenton, S. W. Englander, K. Wuthrich, and A. L. Horwich (2007)
PNAS 104, 20788-20792
   Abstract »    Full Text »    PDF »
From the Cover: Mapping hydration dynamics around a protein surface.
L. Zhang, L. Wang, Y.-T. Kao, W. Qiu, Y. Yang, O. Okobiah, and D. Zhong (2007)
PNAS 104, 18461-18466
   Abstract »    Full Text »    PDF »
Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy.
H. Chen, E. Rhoades, J. S. Butler, S. N. Loh, and W. W. Webb (2007)
PNAS 104, 10459-10464
   Abstract »    Full Text »    PDF »
A backbone-based theory of protein folding.
G. D. Rose, P. J. Fleming, J. R. Banavar, and A. Maritan (2006)
PNAS 103, 16623-16633
   Abstract »    Full Text »    PDF »
The role of hydrophobic interactions in initiation and propagation of protein folding.
H. J. Dyson, P. E. Wright, and H. A. Scheraga (2006)
PNAS 103, 13057-13061
   Abstract »    Full Text »    PDF »
Structural Characterization of Apomyoglobin Self-Associated Species in Aqueous Buffer and Urea Solution.
C. Chow, N. Kurt, R. M. Murphy, and S. Cavagnero (2006)
Biophys. J. 90, 298-309
   Abstract »    Full Text »    PDF »
A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.
P. Bernado, L. Blanchard, P. Timmins, D. Marion, R. W. H. Ruigrok, and M. Blackledge (2005)
PNAS 102, 17002-17007
   Abstract »    Full Text »    PDF »
Influence of Fluoro, Chloro and Alkyl Alcohols on the Folding Pathway of Human Serum Albumin.
Y. Kumar, S. Muzammil, and S. Tayyab (2005)
J. Biochem. 138, 335-341
   Abstract »    Full Text »    PDF »
A protein folding pathway with multiple folding intermediates at atomic resolution.
H. Feng, Z. Zhou, and Y. Bai (2005)
PNAS 102, 5026-5031
   Abstract »    Full Text »    PDF »
Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.
C. Nishimura, H. J. Dyson, and P. E. Wright (2005)
PNAS 102, 4765-4770
   Abstract »    Full Text »    PDF »
The N-terminal to C-terminal motif in protein folding and function.
M. M. G. Krishna and S. W. Englander (2005)
PNAS 102, 1053-1058
   Abstract »    Full Text »    PDF »
Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.
A. M. Bertagna and D. Barrick (2004)
PNAS 101, 12514-12519
   Abstract »    Full Text »    PDF »
Fibrillogenesis and Cytotoxic Activity of the Amyloid-forming Apomyoglobin Mutant W7FW14F.
I. Sirangelo, C. Malmo, C. Iannuzzi, A. Mezzogiorno, M. R. Bianco, M. Papa, and G. Irace (2004)
J. Biol. Chem. 279, 13183-13189
   Abstract »    Full Text »    PDF »
Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of {alpha}-helical content and compactness.
T. Uzawa, S. Akiyama, T. Kimura, S. Takahashi, K. Ishimori, I. Morishima, and T. Fujisawa (2004)
PNAS 101, 1171-1176
   Abstract »    Full Text »    PDF »
Similarity of Force-Induced Unfolding of Apomyoglobin to Its Chemical-Induced Unfolding: An Atomistic Molecular Dynamics Simulation Approach.
H. S. Choi, J. Huh, and W. H. Jo (2003)
Biophys. J. 85, 1492-1502
   Abstract »    Full Text »    PDF »
NMR Elucidation of Early Folding Hierarchy in HIV-1 Protease.
N. S. Bhavesh, R. Sinha, P. M. K. Mohan, and R. V. Hosur (2003)
J. Biol. Chem. 278, 19980-19985
   Abstract »    Full Text »    PDF »
Primary Folding Dynamics of Sperm Whale Apomyoglobin: Core Formation.
M. Gulotta, E. Rogatsky, R. H. Callender, and R. B. Dyer (2003)
Biophys. J. 84, 1909-1918
   Abstract »    Full Text »    PDF »
Characterization of the Unfolding Process of Lipocalin-type Prostaglandin D Synthase.
T. Inui, T. Ohkubo, M. Emi, D. Irikura, O. Hayaishi, and Y. Urade (2003)
J. Biol. Chem. 278, 2845-2852
   Abstract »    Full Text »    PDF »
Tryptophanyl Substitutions in Apomyoglobin Determine Protein Aggregation and Amyloid-like Fibril Formation at Physiological pH.
I. Sirangelo, C. Malmo, M. Casillo, A. Mezzogiorno, M. Papa, and G. Irace (2002)
J. Biol. Chem. 277, 45887-45891
   Abstract »    Full Text »    PDF »
Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain.
M. Maeda, D. Hamada, M. Hoshino, Y. Onda, T. Hase, and Y. Goto (2002)
J. Biol. Chem. 277, 17101-17107
   Abstract »    Full Text »    PDF »
Inaugural Article: An amino acid code for protein folding.
J. Rumbley, L. Hoang, L. Mayne, and S. W. Englander (2001)
PNAS 98, 105-112
   Abstract »    Full Text »    PDF »
The 28-111 disulfide bond constrains the alpha -lactalbumin molten globule and weakens its cooperativity of folding.
Y. Luo and R. L. Baldwin (1999)
PNAS 96, 11283-11287
   Abstract »    Full Text »    PDF »
Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin.
O. Tcherkasskaya and O. B. Ptitsyn (1999)
Protein Eng. Des. Sel. 12, 485-490
   Abstract »    Full Text »    PDF »
Sodium Dodecyl Sulfate Stability of HLA-DR1 Complexes Correlates with Burial of Hydrophobic Residues in Pocket 1.
S. K. Natarajan, L. J. Stern, and S. Sadegh-Nasseri (1999)
J. Immunol. 162, 3463-3470
   Abstract »    Full Text »    PDF »
Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate.
M. S. Kay, C. H. I. Ramos, and R. L. Baldwin (1999)
PNAS 96, 2007-2012
   Abstract »    Full Text »    PDF »
Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol.
T. Knubovets, J. J. Osterhout, P. J. Connolly, and A. M. Klibanov (1999)
PNAS 96, 1262-1267
   Abstract »    Full Text »    PDF »
The N-terminal Sequence Affects Distant Helix Interactions in Hemoglobin. IMPLICATIONS FOR MUTANT PROTEINS FROM STUDIES ON RECOMBINANT HEMOGLOBIN FELIX.
A. Dumoulin, J. C. Padovan, L. R. Manning, A. Popowicz, R. M. Winslow, B. T. Chait, and J. M. Manning (1998)
J. Biol. Chem. 273, 35032-35038
   Abstract »    Full Text »    PDF »
An entropy criterion to detect minimally frustrated intermediates in native proteins.
M. Compiani, P. Fariselli, P. L. Martelli, and R. Casadio (1998)
PNAS 95, 9290-9294
   Abstract »    Full Text »    PDF »
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding.
O. Blum, A. Haiek, D. Cwikel, Z. Dori, T. J. Meade, and H. B. Gray (1998)
PNAS 95, 6659-6662
   Abstract »    Full Text »    PDF »
Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin.
R. Gilmanshin, S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer (1997)
PNAS 94, 3709-3713
   Abstract »    Full Text »    PDF »
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.
M. S. Goldberg, J. Zhang, S. Sondek, C. R. Matthews, R. O. Fox, and A. L. Horwich (1997)
PNAS 94, 1080-1085
   Abstract »    Full Text »    PDF »
Protein Unfolding by Peptidylarginine Deiminase. SUBSTRATE SPECIFICITY AND STRUCTURAL RELATIONSHIPS OF THE NATURAL SUBSTRATES TRICHOHYALIN AND FILAGGRIN.
E. Tarcsa, L. N. Marekov, G. Mei, G. Melino, S.-C. Lee, and P. M. Steinert (1996)
J. Biol. Chem. 271, 30709-30716
   Abstract »    Full Text »    PDF »
Modular Structure of Glucocorticoid Receptor Domains Is Not Equivalent to Functional Independence. STABILITY AND ACTIVITY OF THE STEROID BINDING DOMAIN ARE CONTROLLED BY SEQUENCES IN SEPARATE DOMAINS.
M. Xu, P. K. Chakraborti, M. J. Garabedian, K. R. Yamamoto, and S. S. Simons Jr. (1996)
J. Biol. Chem. 271, 21430-21438
   Abstract »    Full Text »    PDF »
The Radius of Gyration of an Apomyoglobin Folding Intermediate.
D. Eliezer, P. A. Jennings, P. E. Wright, S. Doniach, K. O. Hodgson, and H. Tsuruta (1995)
Science 270, 487
   PDF »
In pursuit of protein folding.
S. Englander (1993)
Science 262, 848-849
   PDF »
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.
P. Jennings and P. Wright (1993)
Science 262, 892-896
   Abstract »    PDF »
Metal ion-dependent modulation of the dynamics of a designed protein.
T. Handel, S. Williams, and W. DeGrado (1993)
Science 261, 879-885
   Abstract »    PDF »
Reexamination of the folding of BPTI: predominance of native intermediates.
J. Weissman and P. Kim (1991)
Science 253, 1386-1393
   Abstract »    PDF »
The Stabilities of Mammalian Apomyoglobins Vary over a 600-Fold Range and Can Be Enhanced by Comparative Mutagenesis.
E. E. Scott, E. V. Paster, and J. S. Olson (2000)
J. Biol. Chem. 275, 27129-27136
   Abstract »    Full Text »    PDF »
Multisite Fluorescence in Proteins with Multiple Tryptophan Residues. APOMYOGLOBIN NATURAL VARIANTS AND SITE-DIRECTED MUTANTS.
O. Tcherkasskaya, V. E. Bychkova, V. N. Uversky, and A. M. Gronenborn (2000)
J. Biol. Chem. 275, 36285-36294
   Abstract »    Full Text »    PDF »
Mapping the Pathways for O2 Entry Into and Exit from Myoglobin.
E. E. Scott, Q. H. Gibson, and J. S. Olson (2001)
J. Biol. Chem. 276, 5177-5188
   Abstract »    Full Text »    PDF »
Structural Characterization of Protein Kinase A as a Function of Nucleotide Binding. HYDROGEN-DEUTERIUM EXCHANGE STUDIES USING MATRIX-ASSISTED LASER DESORPTION IONIZATION-TIME OF FLIGHT MASS SPECTROMETRY DETECTION.
M. D. Andersen, J. Shaffer, P. A. Jennings, and J. A. Adams (2001)
J. Biol. Chem. 276, 14204-14211
   Abstract »    Full Text »    PDF »
The pKa of His-24 in the folding transition state of apomyoglobin.
M. Jamin, B. Geierstanger, and R. L. Baldwin (2001)
PNAS 98, 6127-6131
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)