Structure and Function of Biological Macromolecules
نویسندگان
چکیده
منابع مشابه
NMR studies of structure and function of biological macromolecules (Nobel Lecture).
Nuclear magnetic resonance (NMR) spectroscopy is unique among the methods available for three-dimensional structure determination of proteins and nucleic acids at atomic resolution, since the NMR data can be recorded in solution. Considering that body fluids such as blood, stomach liquid and saliva are protein solutions where these molecules perform their physiological functions, knowledge of t...
متن کاملWater and Biological Macromolecules
1Dipartimento di Fisica and CNISM, Università di Messina, I-98166 Messina, Italy 2Department of Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA 3Dipartimento di Scienze degli Alimenti e dell’ Ambiente, Università di Messina, I-98166 Messina, Italy 4William Fairfield Warren Distinguished Professor; Professor of Physics; Professor of Chemistry; Pro...
متن کاملStructure Determination of Biological Macromolecules in Solution Using NMR spectroscopy
A detailed understanding of the function of a biological macromolecule requires knowledge of its three-dimensional structure. Most atomic-resolution structures of biological macromolecules have been solved either by x-ray diffraction in single crystals or by nuclear magnetic resonance (NMR) in solution. This review surveys the method of NMR structure determination. First a brief introduction to...
متن کاملCrystallography of Biological Macromolecules
Src homology 2 domain-containing protein tyrosine phosphatase [SHP] substrate 1 (SHPS-1), a receptor-type transmembrane glycoprotein whose cytoplasmic region binds and activates the protein tyrosine phosphatases SHP-1 and SHP-2, and thereby modulates multiple cellular functions. Its extracellular region regulates intercellular communication in the neural and immune systems through its associati...
متن کاملCrystallography of Biological Macromolecules
C218 located at the interface between A-band and M-line. It has been shown by Centner et al. [2] that MURF-1, a member of the RING finger proteins, binds to the two Ig-domains A168 and A169 in proximity to the kinase. Thus, its binding might be involved in the regulation of titin kinase. The structure of this tandem Ig domain has been solved. Ig domains, also in titin, are involved in many prot...
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ژورنال
عنوان ژورنال: Kobunshi
سال: 1967
ISSN: 0454-1138,2185-9825
DOI: 10.1295/kobunshi.16.610