Journal ArticleDOI
The physicochemical basis of the functioning of biological membranes: the conformation of valinomycin and its K+ complex in solution.
Vadim T. Ivanov,I. A. Laine,N.D. Abdulaev,L. B. Senyavina,E. M. Popov,Yu.A. Ovchinnikov,M. M. Shemyakin +6 more
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 1969-03-31. It has received 169 citations till now. The article focuses on the topics: Valinomycin & Biological membrane.read more
Citations
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Journal ArticleDOI
Reverse turns in peptides and proteins.
TL;DR: In this article, reverse turns in Peptides and Protein are discussed and discussed in the context of protein synthesis and protein protein synthesis, and a review of the review is given, with a focus on protein synthesis.
Journal ArticleDOI
Ion transport across thin lipid membranes: a critical discussion of mechanisms in selected systems.
D.A. Haydon,Stephen B. Hladky +1 more
TL;DR: In this paper, a review of the role of 1-carriets in the transfer of ions across thin lipid bilayer membranes is presented, focusing on simpler systems, i.e., the lipid-soluble ions, the 1-1 carriets, a simple pore and a substance which prodeces interacting pores.
Journal ArticleDOI
Cyclodepsipeptides as chemical tools for studying ionic transport through membranes
M. M. Shemyakin,Yu.A. Ovchinnikov,Vadim T. Ivanov,V.K. Antonov,E. I. Vinogradova,A.M. Shkrob,G. G. Malenkov,A. V. Evstratov,I. A. Laine,E. I. Melnik,I. D. Ryabova +10 more
TL;DR: The studies have clearly shown the feasibility of using cyclodepsipeptides with predetermined structural and conformational parameters as chemical tools for membrane studies and it is suggested that the principle of conformation-dependent cation binding through iondipole interactions may possibly lie at the basis of the mode of action of systems governing the natural ion permeability in biological membranes.
Journal ArticleDOI
Temperature dependence of amide proton chemical shifts: the secondary structures of gramicidin S and valinomycin.
M. Ohnishi,Dan W. Urry +1 more
TL;DR: The present work, in addition to demonstrating the temperature method for elucidating secondary structure of polypeptides, may be taken as a confirmation of the gramicidin S and valinomycin structures.
References
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Journal ArticleDOI
The structure of monensic acid, a new biologically active compound.
Journal ArticleDOI
Conformational studies of peptide systems. The rotational states of the NH--CH fragment of alanine dipeptides by nuclear magnetic resonance.
TL;DR: The conformation of the 7-membered hydrogen-bonded ring of the dipeptides has been elucidated and an empirically found stereochemical dependence of the constant 3 J NHCH upon the dihedral angle θ of the fragment has served as basis for discussing the possible conformations of the extended form of the Dipeptide molecules in polar solvents.
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Structure of the K+ complex with nonactin, a macrotetrolide antibiotic possessing highly specific K+ transport properties☆
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The physicochemical basis of the functioning of biological membranes: conformational specificity of the interaction of cyclodepsipeptides with membranes and of their complexation with alkali metal ions.
M. M. Shemyakin,Yu.A. Ovchinnikov,Vadim T. Ivanov,V.K. Antonov,A.M. Shkrob,I.I. Mikhaleva,A. V. Evstratov,G. G. Malenkov +7 more
Journal ArticleDOI
The structure-antimicrobial relation for valinomycin depsipeptides.
M. M. Shemyakin,E. I. Vinogradova,Feigina My,N.A. Aldanova,Loginova Ne,I. D. Ryabova,Pavlenko Ia +6 more
TL;DR: Auf Grund eines grossen Vergleichsmaterials wurden die Strukturelemente, die für die antimikrobielle Aktivität der Cyclodepsipeptide nötig sind, ermittelt.
Related Papers (5)
Temperature dependence of amide proton chemical shifts: the secondary structures of gramicidin S and valinomycin.
M. Ohnishi,Dan W. Urry +1 more