HPLC biological macromolecules: Methods and applications
نویسندگان
چکیده
منابع مشابه
Diffraction methods for biological macromolecules. Part A.
diffraction methods for biological macromolecules part a What to say and what to do when mostly your friends love reading? Are you the one that don't have such hobby? So, it's important for you to start having that hobby. You know, reading is not the force. We're sure that reading will lead you to join in better concept of life. Reading will be a positive activity to do every time. And do you k...
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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 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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Carboxypeptidase Y (CPY) inhibitor I from the yeast, consisting of 204 amino acid residues, belongs to the phosphatidylethanolaminebinding protein (PEBP) family. The 2.7 Å crystal structure of the ICPY complex has been solved by molecular replacement [1, 2]. The structure of I consists of a major -type domain and an Nterminal helical segment. I has two CPY-binding sites: the N-terminal inhibito...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1991
ISSN: 0014-5793
DOI: 10.1016/0014-5793(91)80422-y