Skip to main content Accessibility help
×
  • Cited by 7
Publisher:
Cambridge University Press
Online publication date:
July 2014
Print publication year:
2014
Online ISBN:
9781107045224

Book description

Delivering fundamental insights into the most popular methods of molecular analysis, this text is an invaluable resource for students and researchers. It encompasses an extensive range of spectroscopic and spectrometric techniques used for molecular analysis in the life sciences, especially in the elucidation of the structure and function of biological molecules. Covering the range of up-to-date methodologies from everyday mass spectrometry and centrifugation to the more probing X-ray crystallography and surface-sensitive techniques, the book is intended for undergraduates starting out in the laboratory and for more advanced postgraduates pursuing complex research goals. The comprehensive text provides strong emphasis on the background principles of each method, including equations where they are of integral importance to the individual techniques. With sections on all the major procedures for analysing biological molecules, this book will serve as a useful guide across a range of fields, from new drug discovery to forensics and environmental studies.

Reviews

'The book by Hofmann et al. is an invaluable tool for students (and even more advanced practitioners) in the field of experimental biochemistry and biophysics. It covers in considerable detail a variety of methods and provides very clear explanation on how they can be applied and what can be learned during the process. The book is very well illustrated and uses relatively simple language, although never oversimplified. Its particular strength is in covering a number of methods in a single volume, making it a great reference.'

Alexander Wlodawer - Macromolecular Crystallography Laboratory, National Cancer Institute, Maryland

'Methods of Molecular Analysis in the Life Sciences is a much needed overview of the key analytical techniques currently utilized for biomolecule characterization in the life sciences including mass spectrometry, x-ray crystallography and a host of other techniques. The authors do an excellent job of integrating relevant theoretical considerations of each technique alongside important applications in the life sciences. Each section of the book is filled with literature references, links to additional information on the web, as well as key reference data for each technique. The book will no doubt prove to be a valuable resource to those working in the life sciences including both students and researchers alike.'

Kevin Blackburn - Mass Spectrometry Laboratory Manager, North Carolina State University

‘… a text that delivers the fundamental insights into the most popular methods of molecular analysis in a concise and accessible fashion.’

Robert Huber - Max Planck Institute of Biochemistry, from the Foreword

Refine List

Actions for selected content:

Select all | Deselect all
  • View selected items
  • Export citations
  • Download PDF (zip)
  • Save to Kindle
  • Save to Dropbox
  • Save to Google Drive

Save Search

You can save your searches here and later view and run them again in "My saved searches".

Please provide a title, maximum of 40 characters.
×

Contents

References
Bahatyrova, S., Frese, R., Siebert, C. et al. (2004). The native architecture of a photosynthetic membrane. Nature 430, 1058–62.
Berat, R., Remy-Zolghadry, M., Gounou, C. et al. (2007). Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: an efficient platform for cell adhesion. Biointerphases 2, 165–72.
Bettio, A. & Beck-Sickinger, A. (2001). Biophysical methods to study ligand-receptor interactions of neuropeptide Y. Biopolymers 60, 420–37.
Bohr, N. (1913a). On the constitution of atoms and molecules. Philosophical Magazine 26, 857.
Bohr, N. (1913b). On the constitution of atoms and molecules. Philosophical Magazine 26, 476.
Bohr, N. (1913c). On the constitution of atoms and molecules. Philosophical Magazine 26, 1–25.
Boute, N., Jockers, R. & Issad, T. (2002). The use of resonance energy transfer in high-throughput screening: BRET versus FRET. Trends in Pharmacological Sciences 23, 351–4.
Boutet, S., Lomb, L., Williams, G. J. et al. (2012). High-resolution protein structure determination by serial femtosecond crystallography. Science 337, 362–4.
Bragg, W. H. & Bragg, W. L. (1913). The reflexion of X-rays by crystals. Proceedings of the Royal Society A 88, 428–38.
Brakmann, S. & Nöbel, N. (2003). FRET in der Biochemie. Nachrichten aus Chemie, Technik und Laboratorium 51, 319–23.
Bundle, D. & Siguskjold, B. (1994). Determination of accurate thermodynamics of binding by titration microcalorimetry. Methods in Enzymology 247, 288–305.
Chapman, H. N., Fromme, P., Barty, A. et al. (2011). Femtosecond X-ray protein nanocrystallography. Nature 470, 73–7.
Cooper, A. (1999). Thermodynamic analysis of biomolecular interactions. Current Opinion in Chemical Biology 3, 557–63.
Cooper, A. & McAuley, K. E. (1993). Microcalorimetry and the molecular recognition of peptides and proteins. Philosophical Transactions of the Royal Society A 345, 23–35.
Drake, B., Prater, C. B., Weisenhorn, A. L. et al. (1989). Imaging crystals, polymers, and processes in water with the atomic force microscope. Science 243, 1586–9.
Dunitz, J. (1995). Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions. Chemistry & Biology 2, 709–712.
Förster, T. (1948). Zwischenmolekulare Energiewanderung und Fluoreszenz. Annals of Physics 2, 57–75.
Ganchev, D., Rijkers, D., Snel, M., Killian, A. & de Kruijff, B. (2004). Strength of integration of transmembrane alpha-helical peptides in lipid bilayers as determined by atomic force spectroscopy. Biochemistry 43, 14 987–93.
Gill, S. C. & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry 182, 319–26.
Giordano, L., Jovin, T., Irie, M. & Jares-Erijman, E. (2002). Diheteroarylethenes as thermally stable photoswitchable acceptors in photochromic fluorescence resonance energy transfer (pcFRET). Journal of the American Chemical Society 124, 7481–9.
Grandbois, M., Clausen-Schaumann, H. & Gaub, H. (1998). Atomic force microscope imaging of phospholipid bilayer degradation by phospholipase A2. Biophysical Journal 74, 2398–404.
Harkins, W. D. (1952). The Physical Chemistry of Surface Films. New York: Reinhold.
Hénon, S. & Meunier, J. (1991). Microscope at the Brewster angle: direct observation of first-order phase transitions in monolayers. Review of Scientific Instruments 62, 936–9.
Heyduk, T. & Niedziela-Majka, A. (2002). Fluorescence resonance energy transfer analysis of Escherichia coli RNA polymerase and polymerase-DNA complexes. Biopolymers 61, 201–13.
Hinterdorfer, P., Baumgartner, W., Gruber, H. J., Schilcher, K. & Schindler, H. (1996). Detection and localization of individual antibody–antigen recognition events by atomic force microscopy. Proceedings of the National Academy of Sciences, USA 93, 3477–81.
Hofmann, A. & Wlodawer, A. (2002). PCSB – a program collection for structural biology and biophysical chemistry. Bioinformatics 18, 209–10.
Holdgate, G. (2001). Making cool drugs hot: the use of isothermal titration calorimetry as a tool to study binding energetics. BioTechniques 31, 164–84.
Homola, J. (2003). Present and future of surface plasmon resonance biosensors. Analytical and Bioanalytical Chemistry 377, 528–39.
Hönig, D. & Möbius, D. (1991). Direct visualization of monolayers at the air-water interface by Brewster Angle Microscopy. Journal of Physical Chemistry 95, 4590–2.
Kang, J., Piszczek, G. & Lakowicz, J. (2002). Enhanced emission induced by FRET from a long-lifetime, low quantum yield donor to a long-wavelength, high quantum yield acceptor. Journal of Fluorescence 12, 97–103.
Keller, C. & Kasemo, B. (1998). Surface specific kinetics of lipid vesicle adsorption measured with a quartz crystal microbalance. Biophysical Journal 75, 1397–402.
Kimura, C., Maeda, K., Hai, H. & Miki, M. (2002). Ca2+- and s1-induced movement of troponin T on mutant thin filaments reconstituted with functionally deficient mutant tropomyosin. Journal of Biochemistry 132, 345–52.
Klewpatinond, M. & Viles, J. H. (2007). Fragment length influences affinity for Cu2+ and Ni2+ binding to His96 or His111 of the prion protein and spectroscopic evidence for a multiple histidine binding only at low pH. Biochemical Journal 404, 393–402.
Kohl, T., Heinze, K., Kuhlemann, R., Koltermann, A. & Schwille, P. (2002). A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins. Proceedings of the National Academy of Sciences, USA 99, 12 161–6.
Mach, H., Middaugh, C. R. & Lewis, R. V. (1992). Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Analytical Biochemistry 200, 74–80.
Morse, P. M. (1929). Diatomic molecules according to the wave mechanics. II. Vibrational levels. Physics Review 34, 57–64.
Moshinsky, D. J., Ruslim, L., Blake, R. A. & Tang, F. (2003). A widely applicable, high-throughput TR-FRET assay for the measurement of kinase autophosphorylation: VEGFR-2 as a prototype. Journal of Biomolecular Screening 4, 447–52.
Moukhtar, J., Faivre-Moskalenko, C., Milani, P. et al. (2010). Effect of genomic long-range correlations on DNA persistence length: from theory to single molecule experiments. Journal of Physical Chemistry B 114, 5125–43.
Neutze, R., Wouts, R., van der Spoel, D., Weckert, E. & Hajdu, J. (2000). Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 406, 752–7.
Pan, Y., Shan, W., Fang, H. et al. (2013). Annexin-V modified QCM sensor for the label-free and sensitive detection of early stage apoptosis. Analyst 138, 6287–90.
Perczel, A., Park, K. & Fasman, G. (1992). Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide. Analytical Biochemistry 203, 83–93.
Popmintchev, T., Chen, M., Popmintchev, D. et al. (2012). Bright coherent ultrahigh harmonics in the keV x-ray regime from mid-infrared femtosecond lasers. Science 336, 1287–91.
Remington, S. J. (2011). Green fluorescent protein: a perspective. Protein Science 20, 1509–19.
Rhee, H., June, Y., Lee, J. et al. (2009). Femtosecond characterization of vibrational optical activity of chiral molecules. Nature 458, 310–13.
Rice, P., Longden, I. & Bleasby, A. (2000). EMBOSS: The European Molecular Biology Open Software Suite. Trends in Genetics 16, 276–7.
Richter, R. P., Hock, K. K., Burkhartsmeyer, J. et al. (2007). Membrane-grafted hyaluronan films: a well-defined model system of glycoconjugate cell coats. Journal of the American Chemical Society 129, 5306–7.
Rodahl, M., Höök, F., Krozer, A., Brzezinski, P. & Kasemo, B. (1996). Quartz crystal microbalance setup for frequency and Q-factor measurements in gaseous and liquid environments. Review of Scientific Instruments 66, 3924–30.
Rogers, M. S., Cryan, L. M., Habeshian, K. A. et al. (2012). A FRET-based high throughput screening assay to identify inhibitors of anthrax protective antigen binding to capillary morphogenesis gene 2 protein. PLoS ONE 7, e3991.
Rosenblum, B., Lee, L., Spurgeon, S. et al. (1997). New dye-labeled terminators for improved DNA sequencing patterns. Nucleic Acids Research 25, 4500–4.
Salzer, R. & Steiner, G. (2004). Oberflächenplasmonen-Resonanz in neuem Licht. Nachrichten aus Chemie, Technik und Laboratorium 52, 809–11.
Sambrook, J., Fritsch, E. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
Sauerbrey, G. (1959). Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung. Zeitschrift für Phyik 155, 206–22.
Schwartz, C. L., Heumann, J. M., Dawson, S. C. & Hoenger, A. (2012). A detailed, hierarchical study of Giardia lamblia’s ventral disc reveals novel microtubule-associated protein complexes. PLoS ONE 7, e43783.
Simon, A., Cohen-Bouhacina, T., Porte, M. C. et al. (2003). Characterization of dynamic cellular adhesion of osteoblasts using atomic force microscopy. Cytometry 54A, 36–47.
Song, L., Jares-Erijman, E. & Jovin, T. (2002). A photochromic acceptor as a reversible light-driven switch in fluorescence resonance energy transfer (FRET). Journal of Photochemistry and Photobiology A: Chemistry 150, 177–85.
Stryer, L. & Haugland, R. (1967). Energy transfer: a spectroscopic ruler. Proceedings of the National Academy of Sciences, USA 58, 719–26.
Trakselis, M., Alley, S., Abel-Santos, E. & Benkovic, S. (2001). Creating a dynamic picture of the sliding clamp during T4 DNA polymerase holoenzyme assembly by using fluorescence resonance energy transfer. Proceedings of the National Academy of Sciences, USA 98, 8368–75.
Uhlemann, S., Müller, H., Hartel, P., Zach, J. & Haider, M. (2013). Thermal magnetic field noise limits resolution in transmission electron microscopy. Physical Review Letters 111, 046101.
Ullman, E. F., Kirakossian, H., Singh, S. et al. (1994). Luminescent oxygen channeling immunoassay: Measurement of particle binding kinetics by chemiluminescence. Proceedings of the National Academy of Sciences, USA 91, 5426–30.
Warburg, O. & Christian, W. (1941). Isolierung und Kristallisation des Gärungsferments Enolase. Biochemische Zeitschrift 310, 384–421.
White, T. A., Kirian, R. A., Martin, A. V. et al. (2012). CrystFEL: a software suite for snapshot serial crystallography. Journal of Applied Crystallography 45, 335–41.
Wiseman, T., Williston, S., Brandts, J. & Lin, L. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry 179, 131–7.
Xu, Y., Piston, D. & Johnson, C. (1999). A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proceedings of the National Academy of Sciences, USA 96, 151–6.

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Book summary page views

Total views: 0 *
Loading metrics...

* Views captured on Cambridge Core between #date#. This data will be updated every 24 hours.

Usage data cannot currently be displayed.