Proton transfer in and polarizability of hydrogen bonds in proteins. Tyrosine-lysine and glutamic acid-lysine hydrogen bonds ? IR investigations

Kristof, Wolfgang; Zuńdel, Georg

doi:10.1007/bf00537294

Cited by 32 publications

(13 citation statements)

References 33 publications

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“…In fact, when the aligned sequences (Table 3) are examined, two potential hydrogen bonds of this type become immediately apparent: those between lysine 129 and tyrosine 79 on the one hand, and tyrosine 64 and arginine 82 on the other. In fact, neutral, strong hydrogen bonds of this type, in which the proton is retained preferentially by the phenolic oxygen, have been observed directly in lpsinetyrosine co-polymers (Kristof & Zundel, 1980). The biological function of bacteriorhodopsin must also be considered.…”

Section: Discussionmentioning

confidence: 99%

A simple method for displaying the hydropathic character of a protein

Kyte

Doolittle

1982

Journal of Molecular Biology

21,436

256

12,351

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Section: Discussionmentioning

confidence: 99%

A simple method for displaying the hydropathic character of a protein

Kyte

Doolittle

1982

Journal of Molecular Biology

21,436

256

12,351

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“…Considering the evidence on electrostatic and hydrogen bonding interactions in soluble, globular proteins (Thornton, 1982;Rashin and Honig, 1984), in membrane proteins (Engelman, 1982;Kyte and Doolitfle, 1982) and in model compounds (Kristof and Zundel, 1980), it appears plausible that polar residues can exist in environments that have low dielectric constants if extensive networks of hydrogen bonds are formed (Baker and Hubbard, 1984). Such bonds, which would be particularly strong in a medium with a low dielectric constant, may exist between potentially ionizable residues (present as neutral species because of their local environment) and residues such as tyrosine, asparagine, and other hydrogen bond accepting and donating groups.…”

Section: Introductionmentioning

confidence: 99%

Folding patterns of porin and bacteriorhodopsin.

Paul¹,

Rosenbusch²

1985

The EMBO Journal

204

110

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Porin spans the outer membrane of Escheichia coli with most of the protein embedded within the membrane. It lacks pronounced hydrophobic domains and consists predominantly of ,3-pleated sheet. These observations require the acommodation of polar and ionizable residues in an environment that has a low dielectric constant. Owing to a currently limited understanding of the constraints governing membrane protein structure, a miinimal approach to structure prediction is proposed that identifies segments causing polypeptides to reverse their direction (turn identification). The application of this procedure avoids hydrophobicity parameters and yields a model of porin which is in good agreement with all experimental data available. The presence of polar and ionizable residues within membrane boundaries implies a dense (saturating) network of hydrogen bond donor and acceptor groups. Application to a paradigm of hydrophobic membrane proteins, bacteriorhodopsin, reveals a pattern consistent with its a-helical folding. The postulated structure includes significantly more polar residues in the membrane domain than have been assumed previously, suggesting that there are also hydrogen bonding networks in bacteriorhodopsin. Extensive networks permeating protein interior and surfaces would explain the extraordinary stability and the tight interactions between functional units in the formation of crystaline arrays of both proteins.

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“…If the proton is close to the midpoint, it can be easily shifted by electric fields due to the large proton polarizability of such hydrogen bonds. Zundel suggests (197,198) that this is the case, among others, of protonated Schiff baselaspartate or phenolate systems. Hydrogen bonded chains with large proton polarizability could be important for the conduction of the positive charge in bR and in the proton pumping mechanism.…”

Section: Protonation and Hydrogen Bondingmentioning

confidence: 98%

“…The second donor could be another carboxylic acid and more than two may be involved. (See also Denisov and Golubev (205), Zundel and Merz (191), Kristof and Zundel (197,198), and Rosenbusch (129) (64)). …”

Section: Stabilization Of the Ion-pairmentioning

confidence: 99%

The photochemical event in rhodopsins

Sándorfy¹,

Vocelle²

1986

Can. J. Chem.

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. 64, 225 1 (1986).The photochemical step in the functioning of visual and bacterial rhodopsins entails cis-trans or trans-cis isomerization and changes in the state of protonation of the retinylidene Schiff base chromophore. In this review our present knowledge on these two events is discussed as well as the role of interactions between the chromophore and the surrounding protein, opsin. The relation between protonation and hydrogen bonding at the Schiff base nitrogen, the problems of stabilization of the proton bridge and charge separation are also discussed. A new proposal is made which implies Schiff base to counter-ion proton translocation with concomitant isomerization and reprotonation of the chromophore.

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Proton transfer in and polarizability of hydrogen bonds in proteins. Tyrosine-lysine and glutamic acid-lysine hydrogen bonds ? IR investigations

Cited by 32 publications

References 33 publications

A simple method for displaying the hydropathic character of a protein

A simple method for displaying the hydropathic character of a protein

Folding patterns of porin and bacteriorhodopsin.

The photochemical event in rhodopsins

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