The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure<sup>*</sup>

Davidson, Bert J.; Fasman, Gerald D.

doi:10.1021/bi00858a008

Cited by 279 publications

(143 citation statements)

References 59 publications

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“…and c.d. spectrum, has been shown to have the ability to adopt several discrete conformations, dependent upon conditions of pH, ionic strength, and temperature (42)(43)(44)(45)(46)(47)(48)(49). In contrast, the constancy of the c.d.…”

Section: Discussionmentioning

confidence: 99%

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Williams¹,

Kielland²

1975

Can. J. Chem.

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Section: Discussionmentioning

confidence: 99%

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Williams¹,

Kielland²

1975

Can. J. Chem.

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“…Ltd., was turned into a compound with HC1 according t o the known procedure. 6 The silk fibroin was isolated from thc Bombyx mori coccoons and transferred to a water ~olution.~ The proper solution in heavy water was obtained by the additional dialysis against D20 for 1.5 days with heavy water being changed 10 times. After centrifuging the solution was ready.…”

Section: Methodsmentioning

confidence: 99%

Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms

Chirgadze¹,

Shestopalov²,

Venyaminov³

1973

Biopolymers

172

150

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synopsisThe intensities and other spectral parameters of the main components of infrared amide bands for the random and anti-parallel pleated sheet forms have been determined for poly-S-carbobensoxymethylcysteine, poly-8-carboxymethylcysteine, polylysine and silk fibroin of Bombyx mori in heavy water solutions and in organic solvents. Assuming that the optical spectra of these two types of structure are additive, the method was proposed for determining relative contents and molar absorption coefficients of amide I band. Integral intensity and maximum frequency values of the main components of the amide I band for all the samples in the p-form turned out to be specific. In contrast to this the integral intensity of the band of amide I in the random coil form varied within certain limits, while the main maximum frequency for all samples remained the same.

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“…Because of its structural plasticity and ease of manipulation, poly(K) is a good candidate system for modeling the dynamics of the initial protein conformation changes involved in α-helix to β-sheet transitions. At high pH, poly(K) is α-helical and readily converts to β-sheet structure at elevated temperatures (19).…”

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confidence: 99%

Intermediacy of Poly(l-proline) II and β-Strand Conformations in Poly(l-lysine) β-Sheet Formation Probed by Temperature-Jump/UV Resonance Raman Spectroscopy

et al. 2005

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Ultraviolet resonance Raman spectroscopy (UVRR) in combination with a nanosecond temperaturejump (T-jump) was used to investigate early steps in the temperature induced α-helix to β-sheet conformational transition of poly(L-lysine) (poly(K)). Excitation at 197 nm from a tunable frequency-quadrupled Ti:Sapphire laser provided high-quality UVRR spectra, containing multiple conformation-sensitive amide bands. Although unionized poly(K) (pH 11.6) is mainly α-helical below 30°C, there is a detectable fraction (∼15 %) of unfolded polypeptide, which is mainly in the polyproline II (PPII) conformation. However, deviations from the expected amide I and II signals indicate an additional conformation, suggested to be β-strand. Above 30°C unionized poly(K) forms β-sheet at a rate (minutes) which increases with increasing temperature. A 22 -44°C T-jump is accompanied by prompt amide I and II difference signals suggested to arise from a rapid shift in the PPII/β-strand equilibrium. These signals are superimposed on a subsequently evolving difference spectrum which is characteristic of PPII, although the extent of conversion is low, ∼ 2 % at the 3 μs time limit of the experiment. The rise time of the PPII signals is ∼250 ns, consistent with melting of short α-helical segments. A model is proposed in which the melted PPII segments interconvert with β-strand conformation, whose association through inter-strand H-bonding nucleates the formation of β-sheet. The intrinsic propensity for β-strand formation could be a determinant of β-sheet induction time, with implications for the onset of amyloid diseases. KeywordsUVRR; resonance Raman; protein folding; poly(L-lysine); PPII; β-strand; α-helix; β-sheet; temperature-jump; T-jump Several degenerative diseases, including Alzheimer's, Huntington's, Parkinson's, and transmissible spongiform encephalopathies (TSE), are associated with misfolding and aggregation of proteins (1). The misfolded proteins form fibrillous aggregates, termed amyloid fibrils, which have a cross β-sheet structure in which the polypeptide backbone is perpendicular to the fibril axis(2). This allows the fibril to grow lengthwise with the addition of subsequent misfolded protein molecules. It is interesting to note that conditions which promote partial folding of proteins, appear to promote fibril formation in vitro (3)(4)(5). † This work was supported by NIH Grants R01 GM 025158 to T.G.S. and NIH F32 AG 022770 to R.D.J. * To whom correspondence should be addressed: Princeton University, Department of Chemistry, Princeton, NJ, 08544. Telephone: (609) Certain proteins with abundant α-helical structure, including the prion protein (PrP C ) and apomyoglobin, convert to β-sheet rich structures under denaturing conditions (4-6). What is equally provocative is the correlation between metastable α-helices and β-sheet amyloid formation. The β-amyloid (Aβ) peptide involved in Alzheimer's disease and its constituent fragments contain no stable secondary structure in aqueous solutions (7,8), but when the nascent helic...

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The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure^*

Cited by 279 publications

References 59 publications

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms

Intermediacy of Poly(l-proline) II and β-Strand Conformations in Poly(l-lysine) β-Sheet Formation Probed by Temperature-Jump/UV Resonance Raman Spectroscopy

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The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure*

Cited by 279 publications

References 59 publications

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Water-Soluble Lysine-containing Polypeptides. II. The Interaction of Several Sequential Lysine–Glycine Polypeptides with DNA. A Circular Dichroism Study of DNA Conformation in Annealed Complexes

Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms

Intermediacy of Poly(l-proline) II and β-Strand Conformations in Poly(l-lysine) β-Sheet Formation Probed by Temperature-Jump/UV Resonance Raman Spectroscopy

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The Conformational Transitions of Uncharged Poly-L-lysine. α Helix-Random Coil-β Structure^*