The hydration of synthetic polypeptides

Breuer, M. M.; Kennerley, M.

doi:10.1016/0021-9797(71)90272-4

Cited by 34 publications

(7 citation statements)

References 15 publications

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“…The calculations indicate therefore that an a-helical polypeptide with no hydrophilic side chains may nevertheless have associated with it a ' background' level of water bonded to the peptide units. This is supported by experimental measurements (Mellon, Korn & Hoover, 1948;Breuer, 1964) although the nature of the interaction was not clearly understood (Breuer & Kennerley, 1971). Another confirmation of the ability of an already hydrogen-bonded peptide carbonyl to further bind water is seen in the crystal structure of o-bromocarbobenzoxyglycyl-L-prolyl-L-leucyl-glycyl-L-proline ethylacetate monohydrate (Ueki et al 1971) where one carbonyl oxygen which is hydrogenbonded to an NH group accepts another proton from the water molecule.…”

Section: Hydration Sites Of Biomoleculesmentioning

confidence: 87%

“…There is a quantitative spreading among the available experimental results but the trend is clearly indicated (see, for instance, Subramanian & Fischer, 1972;Hnogewyj & Ryerson, 1963). As to the numbers, Breuer & Kennerley (1971) and Kuntz (1971) agree on 2 molecules of water per residue for polyglutamic acid. Allowing one water molecule for the peptide linkage (as found in polyglycine) this leaves one water molecule for complexing with a COOH group.…”

Section: Aliphatic and Aromatic Hydroxyl Groups Hydration Of Ethanolmentioning

confidence: 89%

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New Paths in the Molecular Orbital Approach to Solvation of Biological Molecules

Pullman

1974

Quart. Rev. Biophys.

129

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This review is devoted to the presentation of recent developments in a field of theoretical molecular biophysics which seem to open large possibilities for progress in a hitherto relatively unexplored although very important direction. It is concerned with the establishment of a new methodology in the molecular orbital approach to the problem of the solvation of biological molecules. The methodology is still in an initial stage, susceptible of many refinements and its practical applications may also be considered as being in their beginnings. Nevertheless the successes obtained so far and the interest which they aroused in a number of laboratories incite us to present already now the general principles and the available results so as to offer a possibility of evaluating the advantages, present-day limitations and future potentialities of the procedure, which could then be explored by all those interested. This review may thus be said to be to a large extent oriented towards the future, with the acknowledged aim of producing an acceleration and widening of researches in this field. Possible progress in this respect is interesting from a double point of view.

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Section: Hydration Sites Of Biomoleculesmentioning

confidence: 87%

Section: Aliphatic and Aromatic Hydroxyl Groups Hydration Of Ethanolmentioning

confidence: 89%

New Paths in the Molecular Orbital Approach to Solvation of Biological Molecules

Pullman

1974

Quart. Rev. Biophys.

129

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“…Local effects whereby near-neighbor groups influence the hydration of a given polar group (e.g., see Ref. 44). …”

Section: Cooperativity and Relative Apparent Affinitiesmentioning

confidence: 99%

Sequential hydration of dry proteins: A direct difference IR investigation of sequence homologs lysozyme and α‐lactalbumin

Poole

Finney

1984

Biopolymers

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SynopsisDirect difference ir spectra are presented as a function of hydration for lysozyme and u-lactalbumin, and detailed sequential hydration molecular events identified. Despite the strong sequence homology between the two proteins, and their expected conformational similarity, the hydration behavior of the polar groups is different for the two proteins. Using a Hill-type analysis, we conclude that the acid groups ionize and hydrate rapidly and noncooperatively in both proteins, consistent with the known (lysozyme) and postulated (a-lactalbumin) surface chemistry. The polar group hydration shows a clear cooperativity, which is quantitatively different in the two proteins. Complementary work suggests this cooperativity relates to a hydration-induced "loosening up" of the lysozyme conformation a t about 55 mol water/mol protein. u-Lactalbumin appears to "open up" more easily for hydration than does lysozyme, consistent with its lower stability against thermal and acid denaturation.

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“…This distinction between the proton conductivity at 60% RH and in the fully solvated system arises from changes in the nanotube structure and dynamics. Our MD simulations of the peptide nanotubes under aqueous conditions show significantly larger water absorption and penetration into the peptide nanotubes than is expected at 60% RH based on water adsorption models − and on measurements of the hydration of other amino acid-based systems. − This water penetration influences access to optimal local configurations for PT between amino acid side chains. From a dynamical perspective, the interstitial water molecules between the experimentally observed bundled peptide nanotubes, like water molecules at protein–protein interfaces, − are expected to have much slower dynamics than water molecules surrounding the single, fully solvated peptide nanotubes that are examined in the MD simulations.…”

Section: Resultsmentioning

confidence: 74%

Mechanism of Side Chain-Controlled Proton Conductivity in Bioinspired Peptidic Nanostructures

et al. 2021

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Bioinspired peptide assemblies are promising candidates for use as proton-conducting materials in electrochemical devices and other advanced technologies. Progress toward applications requires establishing foundational structure–function relationships for transport in these materials. This experimental–theoretical study sheds light on how the molecular structure and proton conduction are linked in three synthetic cyclic peptide nanotube assemblies that comprise the three canonical basic amino acids (lysine, arginine, and histidine). Experiments find an order of magnitude higher proton conductivity for lysine-containing peptide assemblies compared to histidine and arginine containing assemblies. The simulations indicate that, upon peptide assembly, the basic amino acid side chains are close enough to enable direct proton transfer. The proton transfer kinetics is determined in the simulations to be governed by the structure and flexibility of the side chains. Together, experiments and theory indicate that the proton mobility is the main determinant of proton conductivity, critical for the performance of peptide-based devices.

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The hydration of synthetic polypeptides

Cited by 34 publications

References 15 publications

New Paths in the Molecular Orbital Approach to Solvation of Biological Molecules

New Paths in the Molecular Orbital Approach to Solvation of Biological Molecules

Sequential hydration of dry proteins: A direct difference IR investigation of sequence homologs lysozyme and α‐lactalbumin

Mechanism of Side Chain-Controlled Proton Conductivity in Bioinspired Peptidic Nanostructures

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