Zobrazeno 1 - 10 of 243 pro vyhledávání: '"V S, Ananthanarayanan"'
1
CD, 1H NMR and molecular modeling studies of the interaction of Ca2+ with substance P and Ala7-substance P in a non-polar solvent
Autor: X F, Qi, B S, Zhorov, V S, Ananthanarayanan
Publikováno v: Journal of peptide science : an official publication of the European Peptide Society. 6(2)
The biologically relevant conformation of substance P is likely to be dictated by the lipid milieu wherein the hormone would interact with its receptor. Assuming that specific constraints to the hormone structure may be imparted by its interaction wi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b5d5b55db7b567b3e3b8fbf691874164
https://pubmed.ncbi.nlm.nih.gov/10718128
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2
Ca2+-dependent antifreeze proteins. Modulation of conformation and activity by divalent metal ions
Autor: K V, Ewart, D S, Yang, V S, Ananthanarayanan, G L, Fletcher, C L, Hew
Publikováno v: The Journal of biological chemistry. 271(28)
The antifreeze proteins (AFPs) are structurally diverse molecules that share an ability to bind to ice crystals and inhibit their growth. The type II fish AFPs of Atlantic herring and smelt are unique among known AFPs in their requirement of a cofact
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::412e64327587dd228481c0a297ee8347
https://pubmed.ncbi.nlm.nih.gov/8663288
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3
Interaction of oxytocin with Ca2+: I. CD and fluorescence spectral characterization and comparison with vasopressin
Autor: V S, Ananthanarayanan, K S, Brimble
Publikováno v: Biopolymers. 40(5)
Extracellular Ca2+ is required for the action of oxytocin and both the hormone and its receptor have binding sites for divalent metal cations. To characterize the cation-bound form of oxytocin, we monitored the binding of Ca2+ and Mg2+ to oxytocin as
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2fc4a1e6706782f8007b87041e52d847
https://pubmed.ncbi.nlm.nih.gov/9062067
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4
Interaction of oxytocin with Ca2+: II. Proton magnetic resonance and molecular modeling studies of conformations of the hormone and its Ca2+ complex
Autor: V S, Ananthanarayanan, M P, Belciug, B S, Zhorov
Publikováno v: Biopolymers. 40(5)
Drastic changes in the CD and fluorescence spectra of oxytocin [cyclo(Cys1-Tyr2-Ile3-Gln4-Asn5-Cys6)-Pro7-Leu8-Gly 9-NH2] occur on binding Ca2+ in trifluoroethanol (Ananthanarayanan and Brimble, preceding paper). To further characterize the conformat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ab6aae852cc4c7ad2732f825b9c85e72
https://pubmed.ncbi.nlm.nih.gov/9062068
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8
Conformational requirement for lysine hydroxylation in collagen. Structural studies on synthetic peptide substrates of lysyl hydroxylase
Autor: P, Jiang, V S, Ananthanarayanan
Publikováno v: The Journal of biological chemistry. 266(34)
An attempt has been made to understand the conformational determinants that govern the hydroxylation of selected lysyl residues in the nascent collagen molecule by lysyl hydroxylase (EC 1.14.11.4). A series of peptide substrates of the enzyme, rangin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7bb9b303b5cb4256feb6e6c82d674793
https://pubmed.ncbi.nlm.nih.gov/1744090
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9
Interaction of prolyl 4-hydroxylase with synthetic peptide substrates. A conformational model for collagen proline hydroxylation
Autor: P L, Atreya, V S, Ananthanarayanan
Publikováno v: The Journal of biological chemistry. 266(5)
With the aim of understanding the structural basis for the substrate specificity of collagen prolyl 4-hydroxylase, we have studied the conformational features of synthetic oligopeptide substrates and their interaction with the enzyme purified from ch
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f81ed26d10e212d5c2fa7f72bfa47842
https://pubmed.ncbi.nlm.nih.gov/1847136
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