Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Molecular chaperones. --- Chaperone proteins --- Chaperones, Molecular --- Chaperonins --- Proteins

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

Chaperonins --- Heat-shock proteins --- Protein degradation --- Protein formation

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

''Excellent and very timely....It will undoubtedly become a standard reference for the application of circular dichroism (CD) to biomolecules.'' --- Quarterly Review of Biology, March 1997 ''[T]estament to the book's utility is the fact that during the course of my review I had to 'rescue' it from the desks of graduate students on an almost daily basis. In summary, this is a great book.'' --- American Scientist ''Well documented chapters provide a very good insight into the problems surrounding the conformation of biomacromolecules...An indispensible source of information.'' --- Nahrung, 42(2), 1998 Renowned experts present the first state-of-the-art description of circular dichroism spectroscopy (CD). Chapters present in-depth discussions of the history of the field, the theory of CD for application to globular proteins, membrane proteins, peptides, nucleic acids and their interactions, carbohydrates, and instrumentation. Discussions also feature new techniques using synchrotron radiation, vibrational Raman optical activity, and vibrational CD. More than 250 illustrations supplement the text.

Biomolecules --- Circular dichroism. --- Conformation. --- CIRCULAR DICHROISM --- CONFORMATION --- PROTEINS --- POLYPEPTIDES --- NUCLEIC ACIDS --- CARBOHYDRATES --- CHAPERONINS --- PROPERTIES

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

The precise shape of a protein is a crucial factor in its function. Molecular chaperones and protein folding catalysts bind to develop proteins in the cell and ensure correct folding and transport. This guide catalogues 200 such molecules.

Molecular chaperones. --- Protein folding. --- Folding of proteins --- Proteins --- Chaperone proteins --- Chaperones, Molecular --- Chaperonins --- Folding --- Conformation --- Catalysts --- Molecular chaperones --- Protein folding

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

In Chaperonin Protocols, Christine Schneider has assembled a unique collection of readily reproducible protocols for the study of chaperonins, intracellular proteins critical to many biological processes. Written by experienced investigators who have successfully honed their methods to a fineness, the protocols focus on the purification of chaperonins from different species along with their corresponding cofactors, and on chaperonin activity assays for in vivo as well as in vitro work. Many activity assays are given for GroEL, which can also be applied to mitochrondrial Hsp60. There are also assays for the eukaryotic chaperonin TRiC and handy methods-for example, one for preparing labeled probes-that can be used for various purposes and prove helpful in numerous different procedures. Critically important to a greater understanding of such disorders as cystic fibrosis, Alzheimer's disease, and BSE, Chaperonin Protocols offers both novice and experienced investigators fast access to today's best and most productive chaperonin methods, all explained in step-by-step detail to ensure robust and reproducible results.

Molecular chaperones --- Purification --- Molecular biology. --- Molecular biochemistry --- Molecular biophysics --- Biochemistry --- Biophysics --- Biomolecules --- Systems biology --- Chaperone proteins --- Chaperones, Molecular --- Chaperonins --- Proteins --- Biochemistry. --- Biochemistry, general. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Composition