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Query: UNIPROT:P01350 (gastrin)
 9,683 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The conformation of some polypeptides and proteins in sodium dodecyl sulfate (NaDodSO4) solutions was studied by circular dichroism. The type and extent of induced structure depend on their helix- and beta-forming potential. Anionic side groups in segments of helix or beta form tend to destabilize the ordered structure unless they are protonated. beta-Endorphin has one Glu inside a predicted helical segment; its helicity in a NaDodSO4 solution is enhanced at pH below 4. alpha-Melanocyte-stimulating hormone having a Glu in a beta segment undergoes a pH-induced coil to beta transition in 1.25 mM NaDodSO4 (excess surfactant will disrupt the beta form). Reduced somatostatin assumes a beta form in 2 mM NaDodSO4 and a partial helix in 25 mM NaDodSO4, both of which are unchanged in acidic pH because it lacks -COOH groups. The unordered gastrin with five consecutive Glu's becomes helical in a NaDodSO4 solution at pH 4. Neurotensin with one Glu has no structure-forming potential and is unordered in both neutral and acidic NaDodSO4 solutions. This charge effect also manifests in segments of ordered structure for polypeptides and proteins such as glucagon, cytochrome c, parvalbumin, ribonuclease A, and lysozyme. The effect is especially predominant in tropomyosin that is rich in clusters of anionic side groups. Its more than 90% helicity is reduced to about one-half in a neutral NaDodSO4 solution, but most of it can be restored by lowering the pH to 2.4.
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PMID:Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. 611 37

The pH dependence of circular dichroism spectra has been studied for dodecyl sulfate complexes formed by 25 proteins and for a random copolypeptide of glutamic acid and alanine. The pH range covered is that in which titration of side-chain carboxyl groups is to be expected. Circular dichroism spectra signify an increase in helical content upon acidification, although in many cases the increase is quite small. For all but three of the proteins studied, the spectral changes are in reasonable agreement with those expected because helix propagation by glutamyl and aspartyl residues is enhanced when the state of the side-chain carboxyl changes from COO- to COOH. This simple explanation seriously underestimates conformational changes reported for gastrin, Kunitz trypsin inhibitor and tropomyosin. Changes in charge density appear to play an important role in these proteins.
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PMID:Helix formation upon acidification of protein-dodecyl sulfate complexes. 682 4