1989
DOI: 10.1146/annurev.bb.18.060189.000245
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Expanding Roles of Computers and Robotics in Biological Macromolecular Research

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Cited by 24 publications
(22 citation statements)
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References 87 publications
(110 reference statements)
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“…Recently, Collet et al [13] determined the redox potential of DsbDγ to be −241 mV, which was substantially different from that of E. coli thioredoxin (−270 mV). Since the magnitude of the helix dipole is correlated with the length of the helix [27], the longer active site helix α2a in DsbDγ should stabilize the active site cysteine thiolate more and shift the redox potential towards the oxidizing direction.…”
Section: Resultsmentioning
confidence: 99%
“…Recently, Collet et al [13] determined the redox potential of DsbDγ to be −241 mV, which was substantially different from that of E. coli thioredoxin (−270 mV). Since the magnitude of the helix dipole is correlated with the length of the helix [27], the longer active site helix α2a in DsbDγ should stabilize the active site cysteine thiolate more and shift the redox potential towards the oxidizing direction.…”
Section: Resultsmentioning
confidence: 99%
“…1,2 It is known that peptides with ␣-helical structures possess a large dipole moment created by the sum of the small dipoles of amino acid repeats. 3,4 Electrical studies on peptide monolayer have examined the effects of dipole direction, [5][6][7] linkers, 8,9 chain length, 10 and side chains. 8 These studies have confirmed electron transfer through the ␣-helical peptide monolayer, with the most efficient transfer occurring in the direction from the C-to N-terminus of the molecular axis, which coincides with the internal electric field generated by the ␣-helical dipole.…”
mentioning
confidence: 99%
“…Based on the SEM side view image, the molecular chain at the center of the bundle in the Q t-PBLG film was ϳ110 nm in length, corresponding to ϳ730 amino acid repeats ͑0.15 nm/ residue along the molecular axis͒, resulting in an unprecedented, huge dipole moment of ϳ2550 D ͑3.5 D / residue͒ along the surface normal. 3 As a result, the electron transport efficiency was highly enhanced. As shown in Fig.…”
mentioning
confidence: 99%
“…In a photosynthesis system, vectorial electron transfer can be generated by a vertically oriented α‐helical peptide bundle whose particular functional groups are located in the membrane . The α‐helical peptide has attracted much attention as a universally functional molecule in biological electron‐transfer systems, because the macro‐dipole moment along the helix axis is large, about 3.5 D per amino‐acid residue . Especially in an oriented macro‐dipole moment assembly, effective unidirectional electron transfer is expected.…”
Section: The Calculated Results Of Conformation and Tilt Angles For Tmentioning
confidence: 99%