Size and Shape of Protein Molecules at the Nanometer Level Determined by Sedimentation, Gel Filtration, and Electron Microscopy
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Richards F. M. (1974) The interpretation of protein structures: total volume, group volume distributions and packing density. J Mol Biol 82:1–14
Gittes F., Mickey B., Nettleton J., Howard J. (1993) Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J Cell Biol 120:923–934
Sober H.A. (1966) Handbook of Biochemistry. The Chemical Rubber Co., Cleveland, OH
Siegel L. M., Monte K. J. (1966) Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Biochim Biophys Acta 112:346–362
Hesterberg L. K., Lee J. C., Erickson H. P. (1981) Structural properties of an active form of rabbit muscle phosphofructokinase. J Biol Chem 256:9724–9730
Teller D. C., Swanson E., De Haen C. (1979) The translational friction coefficient of proteins. Methods Enzymol 61:103–124
Garcia De La Torre J., Huertas M. L., Carrasco B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78:719–30
Schürmann G., Haspel J., Grumet M., Erickson H. P. (2001) Cell adhesion molecule L1 in folded (horseshoe) and extended conformations. Mol Biol Cell 12:1765–73
Kirkwood J. G. (1954) The general theory of irreversible processes in solutions of macromolecules. J Polymer Sci 12:1–14
Bloomfield V., Dalton W. O., van Holde K. E. (1967) Frictional coefficients of multisubunit structures. I. Theory. Biopolymers 5:135–148
Carrasco B., Garcia de la Torre J. (1999) Hydrodynamic properties of rigid particles: comparison of different modeling and computational procedures. Biophys J 76:3044–57
Garcia de la Torre J., Llorca O., Carrascosa J. L., Valpuesta J. M. (2001) HYDROMIC: prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron microscopy images. Eur Biophys J 30:457–62
Byron O. (2008) Hydrodynamic modeling: the solution conformation of macromolecules and their complexes. Methods Cell Biol 84:327–73
Schuster T. M., Toedt J. M. (1996) New revolutions in the evolution of analytical ultracentrifugation. Curr Opin Struct Biol 6:650–658
Hansen J. C., Lebowitz J., Demeler B. (1994) Analytical ultracentrifugation of complex macromolecular systems. [Review]. Biochemistry 33:13155–13163
Hall C. E., Slayter H. S. (1959) The fibrinogen molecule: its size, shape, and mode of polymerization. J Biophys Biochem Cytol 5:11–6
Fowler W. E., Erickson H. P. (1979) Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol 134:241–249
Shotton D. M., Burke B. E., Branton D. (1979) The molecular structure of human erythrocyte spectrin. J Mol Biol 131:303–329
Melby T. E., Ciampaglio C. N., Briscoe G., Erickson H. P. (1998) The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge. J Cell Biol 142:1595–1604
Erickson H. P., Fowler W. E. (1983) Electron microscopy of fibrinogen, its plasmic fragments and small polymers. Ann N Y Acad Sci 408:146–163
Erickson H. P., Iglesias J. L. (1984) A six-armed oligomer isolated from cell surface fibronectin preparations. Nature 311:267–269
Zhao F. Q., Craig R. (2003) Capturing time-resolved changes in molecular structure by negative staining. J Struct Biol 141:43–52
Ohi M., Li Y., Cheng Y., Walz T. (2004) Negative staining and image classification—powerful tools in modern electron microscopy. Biol Proced Online 6:23–34
Miranda J. J., De Wulf P., Sorger P. K., Harrison S. C. (2005) The yeast DASH complex forms closed rings on microtubules. Nat Struct Mol Biol 12:138–43
Westermann S., Avila-Sakar A., Wang H. W., Niederstrasser H., Wong J., Drubin D. G., Nogales E., Barnes G. (2005) Formation of a dynamic kinetochore–microtubule interface through assembly of the Dam1 ring complex. Mol Cell 17:277–90
Wang H. W., Ramey V. H., Westermann S., Leschziner A. E., Welburn J. P., Nakajima Y., Drubin D. G., Barnes G., Nogales E. (2007) Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms. Nat Struct Mol Biol 14:721–6
Aukhil I., Joshi P., Yan Y., Erickson H. P. (1993) Cell- and heparin-binding domains of the hexabrachion arm identified by tenascin expression proteins. J Biol Chem 268:2542–2553
Leahy D. J., Axel R., Hendrickson W. A. (1992) Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 Å resolution. Cell 68:1145–1162
Chen S. C., Kramer G., Hardesty B. (1989) Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes. J Biol Chem 264:7267–75