Charge and strangeness transfer in multiparticle production

Robson, D.; Michael, C.

doi:10.1016/0550-3213(76)90151-6

Cited by 16 publications

(20 citation statements)

References 5 publications

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“…Consequently, parameters indicating the free energy gain for a side chain during transition from a random coil in water to a membrane-embedded a-helix (von Heijne, 1981) predict membrane-solubility for two segments of the mature proteolipid only, but not for the presequence (Figure 5). Various prediction methods (Chou and Fasman, 1978;Nagano, 1977;Robson and Suzuki, 1976;Maxfield and Scheraga, 1976) were applied to calculate secondary structure elements of the preproteolipid from the amino acid sequence. a-Helical regions and fl-turns predicted by all four programs are included in the upper part of Figure 5.…”

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confidence: 99%

The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA.

Viebrock¹,

Perz²,

Sebald³

1982

The EMBO Journal

207

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The proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa is an extremely hydrophobic protein of 81 amino acid residues, which is imported into mitochondria as a precursor of mol. wt. 15 000. The primary structure of the imported form has now been determined by isolating and analyzing cDNA clones of the preproteolipid mRNA. An initial cDNA clone was identified by hybridizing total polyadenylated RNA to pooled cDNA recombinant plasmids from an ordered clone bank and subsequent cell‐free translation of hybridization‐selected mRNA. Further preproteolipid clones were identified at a frequency of 0.2% by colony filter hybridization. One isolated cDNA represented the major part of the preproteolipid mRNA. The nucleotide sequence showed 243 bases corresponding to the mature proteolipid and, in addition, 178 bases coding for an amino‐terminal presequence . Non‐coding sequences of 48 bases at the 5′ end and of 358 bases at the 3′ end plus a poly(A) tail were determined. The long presequence of 66 amino acids is very polar, in contrast to the lipophilic mature proteolipid, and includes 12 basic and no acidic side chains. It is suggested that the presequence is specifically designed to solubilize the proteolipid for post‐translational import into the mitochondria.

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mentioning

confidence: 99%

The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA.

Viebrock¹,

Perz²,

Sebald³

1982

The EMBO Journal

207

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“…This strand comprised the glycine-rich pyrophosphatebinding sequence. Predictions of secondary structure using the methods of Chou and Fasman [2] and Robson and Suzuki [3] led to patterns of CZhelix and &sheet without apparent homology to dehydrogenases of known structure.…”

Section: Resultsmentioning

confidence: 99%

“…Pure predictions of protein structure usuaIly try to follow the hierarchic pathway [l]. From the known primary structure, the secondary structure is predicted first [2,3]. These methods yield correct structural predictions for about two-thirds of the amino acids [4}.…”

Section: Introductionmentioning

confidence: 99%

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An integrated prediction of secondary, tertiary and quaternary structure of glucose dehydrogenase

et al. 1987

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Based on homology of partial sequences, on physico~hemi~al evidence and on studies using chemical modification, we came to the tentative conclusion that tetrameric glucose dehydrogenases from Bacillus megaterium and B. subtilis should have a structure closely related to that of lactate dehydrogenase. The overall homology of primary structures was found to be very low, however, and independent predictions of secondary structure produced a clearly different pattern of p-strands and cr-helices. We nevertheless tried a manual prediction based on the hydrophobic nature of internal B-sheet and on the amphiphili~ character of external helices. This treatment led to the identification of analogues of all the b-strands present in lactate dehydrogenase with the exception of j-X. Six amphiphilic helices were identified corresponding to uB, ctC, uD, cllF, u2F and a3G in lactate dehydrogenase. Conserved functional residues were found at analogous positions. The Q and R intersubunit contacts could be identified and partial proteolysis was found to occur on the outer surface of the tetramer. The structure was found to explain the better binding of NADP as compared to NAD' and offered a rationalization of the role of the essential lysine at position 201.

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“…2) the unusual, greater-than-random Occurrence of E R structure over the long interval i -3 I j I i + 1, and the strong preference for A, bends at j = i. 5. Phenylalanine.…”

Section: Appendixmentioning

confidence: 99%

Differential geometry and protein conformation. V. Medium‐range conformational influence of the individual amino acids

Rackovsky

Goldstein

1987

Biopolymers

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SynopsisA previous differential geometric analysis of the conformational properties of the various amino acids has been extended to study their influence on folding over a larger backbone interval. In addition, statistical effects associated with variation in the number of the individual amino acids in the database have been treated in greater detail, using a simulation method. It is found that the amino acids can be divided into three groups on the basis of their conformational influence over four-C" units in the interval i -6 < j s i + 6. Group Ia is composed of .seven amino acids (His, Leu, Ala, Met, Lys, Gln, Ile) that encourage the formation of AR-helical structure. Group Ib (Glu, Phe, Trp, Val, Asp) is composed of amino acids with some helix-forming tendency but that also show positive extended-strand formation tendency. They therefore act BS a bridge between group Ia and group I1 (Cys, Gly, Asn, Pro, Arg, Ser, Thr, Tyr) that contains amino acids that encourage the formation of extended structure and bends. The detailed four-C" con formational properties of each of the amino acids are shown, and the ability of amino acids to exert conformational influence in both directions along the backbone is examined. It is shown that, in general, such influence extends farther in the N-terminal direction than in the C-terminal direction. A framework is briefly sketched for using the present data to investigate actual folding mechanisms.

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Charge and strangeness transfer in multiparticle production

Cited by 16 publications

References 5 publications

The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA.

The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA.

An integrated prediction of secondary, tertiary and quaternary structure of glucose dehydrogenase

Differential geometry and protein conformation. V. Medium‐range conformational influence of the individual amino acids

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