Peptides as Probes in Muscle Research by Johann Caspar Rüegg (auth.), Professor Dr. Johann Caspar

By Johann Caspar Rüegg (auth.), Professor Dr. Johann Caspar Rüegg (eds.)

Protein-protein interactions are inquisitive about muscle contraction and sign transduction. This e-book describes how artificial peptides can be used, very like antibodies, either as particular inhibitors and as molecular probes to discover the cognitive interfaces among interacting proteins and their useful importance. this gives the chance of very selective intervention in mobile mechanisms. those well timed contributions through numerous specialists will attract the researchers in muscle body structure, cardiovascular pharmacology and mobile biology who're attracted to this new approach.

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Biophys Hung 22 (2-3) 307-316 Green LE (1984) Stoichiometry of actin Sl crosslinked complex. J BioI Chern 259:7363-7366 Heaphey S, Tregar R (1984) Stoichiometry of covalent actin-subfragment 1 complexes formed on reaction with a zero-length crosslinking compound. Biochemistry 23:2211-2214 Ikkai T, Wahl P, Auchet J (1979) Anisotropy decay oflabelled actin, evidence of the flexibility of the peptide chain in F-actin molecules. Eur. J. Biochem. 93:397-408 Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (1990) Atomic structure of Actin: DNAase 1 complex.

8 ~M were used. complex. peptides As shown in Table I, the dissociation constants of (1) and (2) had almost the same values. The dissociation constants of peptides (3) and (4) also had values similar to each other. The N-terminal extra tetrapeptide segment of peptides (1) and (3), Val-Leu-Glu-Gly, does not appear to contribute significantly to the binding with F-actin. Therefore, the heptapeptide, peptide (2), is critical for this binding. In this heptapeptide, the N-terminal Ile-Arg-Ile segment appears to be more important for the binding with Factin than the C-terminal Cys-Arg-Lys-Gly segment since the affinity for F-actin of tripeptide (4) was about 10 times higher than that of tetrapeptide (5).

Acad. Sci. USA 85:7471-7475 Elzinga M, Collins JH (1977) Amino acid sequence of a myosin fragment that contains SH-l, SH-2, and N-methylhistidine. Proc. Natl. Acad. Sci. USA 74: 4281-4284 Eto M, Suzuki R, Morita F, Kuwayama H, Nishi N, Tokura S (1990) Roles of the amino acid side chains in the actin-binding Ssite of myosin heavy chain. J. Biochem. 108: 499-504 Garboczi DN, Fox AH, Gerring SL, Pedersen PL (1988) S-subunit of rat liver mitochondrial ATP synthase: cDNA cloning, amino acid sequence, expression in Escherichia coli, and structural relationship to adenylate kinase.

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