Folding of the nascent peptide chain into a biologically active protein

Tsou, Chen‐Lu

doi:10.1021/bi00406a001

Cited by 65 publications

(44 citation statements)

References 41 publications

(45 reference statements)

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“…The N-terminal fragments have been proposed to have similar structural characteristics as the nascent polypeptide when it is synthesized from the N-terminal in ribosome [1]. Examination of the development of the polypeptide chain structure as the C-terminal increases would help to understand how the nascent polypeptide folds in vivo [1].…”

Section: Discussionmentioning

confidence: 99%

“…Examination of the development of the polypeptide chain structure as the C-terminal increases would help to understand how the nascent polypeptide folds in vivo [1]. Studies on the N-terminal fragments of chymotrypsin inhibitor 2, which approaches the minimum structure module, showed that its folding process is concerted and highly cooperative [35].…”

Section: Discussionmentioning

confidence: 99%

“…The mechanisms by which proteins fold to a native state remain a challenging question for biologists [1]. The structure and dynamics of folding intermediates have long been of interest because of the relevance of their conformations to the protein folding pathways.…”

Section: Introductionmentioning

confidence: 99%

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Interactions between subdomains in the partially folded state of staphylococcal nuclease

Ye¹,

Jing²,

Wang³

2000

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Interactions between subdomains in the partially folded state of staphylococcal nuclease

Ye¹,

Jing²,

Wang³

2000

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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“…There are experimental data that support both of the hypotheses (Tsu, 1988;Fredman, 1992).The most convincing arguments for the independence of folding on the direction of biosynthesis are the following: …”

mentioning

confidence: 91%

Structural argument for N‐terminal initiation of protein folding

Alexandrov

1993

Protein Science

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Itis not yet clear whether proteins fold during biosynthesis or whether translation and folding are separated in time. There are experimental data that support both of the hypotheses (Tsu, 1988;Fredman, 1992).The most convincing arguments for the independence of folding on the direction of biosynthesis are the following: 1. 2. 3.Many proteins can be denatured and then refolded again. From this it was concluded that the direction of the biosynthesis is not important for protein structure formation, which is determined only by amino acid sequence. It was shown for several proteins that permutations in sequence do not affect the final structure. In these experiments, edges of a polypeptide chain were artificially linked and then cut in different sites. This permutation replaced the terminal regions without changing other parts of the sequence. In spite of the different order of synthesis, the fold is retained. Some proteins cannot be folded properly without the C-terminal portion.To support the idea that proteins fold simultaneously with .the biosynthesis, one should consider that:Speed of the biosynthesis is several amino acids per second, and this leaves enough time for folding of the partially synthesized protein. At the same time, protein activity can be detected within a few minutes after the initiation of translation, but refolding of completely denatured large proteins requires many minutes or even hours.

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“…These residues do not play a direct role in the folding topology of the peptide or in its interaction with mAb TP25.99. Their presence in the sequence may, however, allow for the peptide structure to occur by providing extra length to the peptide without inducing or stabilizing other viable conformations (1,35).…”

Section: Functional and Sequence Mimicry By The Induced Conformationsmentioning

confidence: 99%

Analysis by NMR Spectroscopy of the Structural Homology between the Linear and the Cyclic Peptide Recognized by Anti-human Leukocyte Antigen Class I Monoclonal Antibody TP25.99*

Moy¹,

Desai²,

Wang³

et al. 2000

Journal of Biological Chemistry

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The anti-human leukocyte antigen (HLA) class I monoclonal antibody (mAb) TP25.99 has a unique specificity since it recognizes both a conformational and a linear determinant expressed on the ␤ 2 --associated and ␤ 2 --free HLA class I heavy chains, respectively. Previously, we reported the identification of a cyclic and a linear peptide that inhibits mAb TP25.99 binding to the ␤ 2 --associated and ␤ 2 --free HLA class I heavy chains (S. A. Desai, X. Wang, E. J. Noronha, Q. Zhou, V. Rebmann, H. Grosse-Wilde, F. J. Moy, R. Powers, and S. Ferrone, submitted for publication). The linear X 19 and cyclic LX-8 peptides contain sequence homologous to residues 239 -242, 245, and 246 and to residues 194 -198, respectively, of HLA class I heavy chain ␣ 3 domain. Analysis by twodimensional transfer nuclear Overhauser effect spectroscopy of the induced solution structures of the linear X 19 and cyclic LX-8 peptides in the presence of mAb TP25.99 showed that the two peptides adopt a similar structural motif despite the lack of sequence homology. The backbone fold is suggestive of a short helical segment followed by a tight turn, reminiscent of the determinant loop region (residues 194 -198) on ␤ 2 --associated HLA class I heavy chains. The structural similarity between the linear X 19 and cyclic LX-8 peptides and the lack of sequence homology suggests that mAb TP25.99 predominantly recognizes a structural motif instead of a consensus sequence. HLA1 class I antigens present peptides to cytotoxic lymphocytes and thus play a crucial role in allograft rejection and tumor surveillance. Like their counterparts in other animal species, HLA class I antigens are comprised of a polymorphic heavy chain non-covalently associated with ␤ 2 -. The association of ␤ 2 -to HLA class I heavy chains causes marked changes in their conformation and in their antigenic profile. This finding, with a few exceptions (2, 3), accounts for the selective reactivity of monoclonal and polyclonal allo-and xenoantibodies with either ␤ 2 --free or ␤ 2 --associated HLA class I heavy chains. In the course of the analysis of the fine specificity of a panel of anti-HLA class I mAb, we have found that mAb TP25.99 has the unusual characteristic to react with both ␤ 2 --free and ␤ 2 --associated HLA class I heavy chains (4, 5). As described in a related paper, 2 this reactivity is mediated by the recognition of distinct and spatially distant antigenic determinants located in HLA class I heavy chain ␣ 3 domains. One expressed on ␤ 2 --associated HLA class I heavy chains has been mapped to amino acid residues 194 -198, and the other one expressed on ␤ 2 --free HLA class I heavy chains has been mapped to amino acid residues 239 -242, 245, and 246. The two antigenic determinants have no homology in their amino acid sequence.Since only the x-ray structure of ␤ 2 --associated HLA class I heavy chain (6, 7) has been described, the structural relationship between the two antigenic determinants in the ␤ 2 --free and ␤ 2 --associated HLA class I heavy chains is not known. To obt...

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Folding of the nascent peptide chain into a biologically active protein

Cited by 65 publications

References 41 publications

Interactions between subdomains in the partially folded state of staphylococcal nuclease

Interactions between subdomains in the partially folded state of staphylococcal nuclease

Structural argument for N‐terminal initiation of protein folding

Analysis by NMR Spectroscopy of the Structural Homology between the Linear and the Cyclic Peptide Recognized by Anti-human Leukocyte Antigen Class I Monoclonal Antibody TP25.99*

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