The C-peptide helix from ribonuclease A considered as an autonomous folding unit.
The C-peptide helix from ribonuclease A considered as an autonomous folding unit.
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来自核糖核酸酶 A 的 C 肽螺旋被视为自主折叠单元。
DOI:
10.1101/sqb.1987.052.01.045
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发表时间:
1987
期刊:
影响因子:
--
通讯作者:
Baldwin,RL
中科院分区:
文献类型:
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作者:
Shoemaker,KR;Fairman,R;Kim,PS;York,EJ;Stewart,JM;Baldwin,RL
One of the basic goals of work on the mechanism of protein folding is to define autonomous folding units: those individual segments of a protein which, if excised, contain sufficient structural information to specify their own folding. Surprisingly little is known about this subject. A common opinion is that entire domains are the units of folding. A domain is defined as (1) a continuous segment of polypeptide chain that is folded on itself, as judged by inspection of the protein's X-ray structure, and (2) a folded segment that makes only marginal contacts with neighboring segments. Domains are usually found to contain 100-150 amino acid residues. The nature of protein structure is such that a domain can be divided into two subdomains and each subdomain can be further divided, if the definition of a subdomain is based on part 1 above (Rose 1979), without part 2.Autonomous folding units might, however, prove to be substantially smaller than entire domains. Gilbert's hypothesis that new proteins can be made by reshuffling exons (Gilbert 1978, 1985) implies that each exon product is an autonomous folding unit (cf. G5 1981) and the peptide segments encoded by exons are often as small as 30-40 residues. The definition of an autonomous folding unit is tied to the criteria used for stability of the folded structure. Our criteria for an autonomous folding unit are as follows:(1) The structure shown by the excised fragment should be sufficiently stable in aqueous solution to be detected, and should occur by a monomolecular reaction.(2) This structure must closely resemble the structure in the intact protein.