Solvent perturbation studies and analysis of protein and model compound data in denaturing organic solvents

Solli, Nicholas J.; Herskovits, Theodore T.

doi:10.1016/0003-2697(73)90365-5

Cited by 19 publications

(10 citation statements)

References 18 publications

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“…Changes in the environment around chromophoric residues in proteins caused by denaturation or solvent perturbation could lead to shifts in the peaks of the absorption spectrum to shorter wavelength (Solli and Herskovits, 1973). The blue shift was slight at 100 "C but quite significant at 110 "C, indicating that oat globulin was not extensively denatured at 100 "C. This is consistent with the exceptionally high thermal stability of oat globulin with a denaturation temperature near 110 "C (Ma and Harwalkar, 1984).…”

Section: Resultssupporting

confidence: 56%

Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

Yung¹,

Harwalkar²

1988

J. Agric. Food Chem.

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Section: Resultssupporting

confidence: 56%

Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

Yung¹,

Harwalkar²

1988

J. Agric. Food Chem.

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“…The observed molecular weights of peptides I, II, III, and IV were 2321.5 (theoretical value, 2321.5), 3749.2 (3749.2), 4927.6 (4928.4), and 3809.0 (3809.3), respectively. The concentrations of the peptide solutions were determined with the absorbance at 280 nm on the basis of absorption coefficients (Solli et al, 1973).…”

Section: Methodsmentioning

confidence: 99%

Identification of Kinesin Neck Region as a Stable α-Helical Coiled Coil and Its Thermodynamic Characterization

et al. 1997

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The kinesin heavy chain consists of an N-terminal globular domain, referred to as the motor domain, a rod-like middle region, and a C-terminal domain. In this study, the human kinesin neck region, the region adjacent to the motor domain which promotes dimerization, has been investigated. First, we predicted coiled-coil regions including the neck region by our newly devised statistical method. The sequence (335-372) was predominated by a unique heptad amphipathy. A comparison of the bacterially expressed human kinesin heavy chain fragments, K349 (1-349), a monomeric motor domain, and K379 (1-379), a dimer, by circular dichroism (CD) spectroscopy showed that K379 had more alpha-helical content. Chemically synthesized peptides, (332-349), (350-379), and (332-369), gave CD spectra with an alpha-helix-rich pattern, but the spectra varied depending on the peptide concentration. Analysis of the molar ellipticity at 222 nm indicated that those peptides were in monomer-dimer equilibria, and the dissociation isotherms established dissociation constants of 9.6 mM. 60 microM, and 62 nM for the above peptides, respectively. Sedimentation equilibrium measurements verified that the peptide (332-369) existed as a dimeric form. These results strongly suggest that the sequence from 332 to 369 of the neck region forms an alpha-helical coiled coil. The differential peptide of K349 and K379, (350-379), did not show sufficient ability to make K379 dimeric. It is likely that the region (350-379) forms a stable alpha-helical coiled coil only together with the (332-349) region. Fluorescence energy transfer studies of [Cys363]-(332-369) labeled with a fluorescence donor and an acceptor revealed that the peptide formed a parallel coiled coil. This coiled coil was thermodynamically stable against urea and thermal denaturation, and peptide exchange of the coiled coil was undetectable, or extremely slow, at neutral pH. The dissociation free energy was estimated to be 57.7 kJ mol-1 at a peptide concentration of 22 microM. These results indicate that the neck region of kinesin forms a stable coiled coil which may be important for the motility of dimeric kinesin.

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“…This procedure yielded a preparation which appeared homogeneous in two different systems of analytical RP-HPLC [5]. Concentrations of peptide solutions in methanol were determined by absorbance determination at 278 nm (ε 278 3340 M L −1 ) [19][20][21][22]. The egg PC was obtained according to [23].…”

Section: Chemicalsmentioning

confidence: 99%

Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers

Bellomio

Oliveira

Maggio

et al. 2005

Journal of Colloid and Interface Science

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Solvent perturbation studies and analysis of protein and model compound data in denaturing organic solvents

Cited by 19 publications

References 18 publications

Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

Identification of Kinesin Neck Region as a Stable α-Helical Coiled Coil and Its Thermodynamic Characterization

Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers

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