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encoded polypeptide. An analysis of the complementation data further indicated that the polypeptides making up the multimer were folded back on themselves in the form of a hairpin. A further high-resolution crystal structure analysis of the distal tail fiber indicated that the gene
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of a particular gene, the mixed multimer may exhibit greater functional activity than the unmixed multimers formed by each of the mutants alone. When a mixed multimer displays increased functionality relative to the unmixed multimers, the phenomenon is referred to as
33:), a sliding DNA clamp protein that is part of the DNA replication complex and serves as a processivity factor for DNA polymerase. The three individual polypeptide chains that make up the trimer are shown.
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Bartual SG, Otero JM, Garcia-Doval C, et al. Structure of the bacteriophage T4 long tail fiber receptor-binding tip. Proc Natl Acad Sci U S A. 2010;107(47):20287-20292.
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Bernstein H, Edgar RS, Denhardt GH. Intragenic complementation among temperature sensitive mutants of bacteriophage T4D. Genetics. 1965;51(6):987-1002.
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and mutants defective in this gene undergo intragenic complementation. This finding indicated that the distal tail fibers are a multimer of the gene
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units help to stabilize the quaternary structure. Since a protein trimer is composed of multiple polypeptide subunits, it is considered an
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polypeptides are present as a trimer and that each polypeptide of the trimer is folded back on itself in a hairpin configuration.
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often can form an aggregate referred to as a multimer. When a multimer is formed from polypeptides produced by two different
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is an example of homotrimeric protein, while Type I collagen is an AAB-type heterotrimeric protein.
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Crick FH, Orgel LE. The theory of inter-allelic complementation. J Mol Biol. 1964 Jan;8:161-5.
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would be formed by three different macromolecules. Type II
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Elsevier's
Integrated Review Biochemistry (Second Edition)
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Pelley, John W. (2012-01-01), Pelley, John W. (ed.),
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Macromolecular complex formed by three macromolecules
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usually arrange themselves in membranes as trimers.
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123:Multiple copies of a polypeptide encoded by a
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72:The non-covalent interactions between the
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139:. The distal portion of each of the
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239:"3 - Protein Structure and Function"
97:would be formed by three identical
348:. You can help Knowledge (XXG) by
251:10.1016/b978-0-323-07446-9.00003-9
209:10.1016/b978-1-907568-28-2.00002-2
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201:An Introduction to Biotechnology
143:tail fibers is encoded by gene
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284:10.1016/s0022-2836(64)80156-x
171:Protein quaternary structure
203:, Elsevier, pp. 9–33,
119:Bacteriophage T4 tail fiber
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137:intragenic complementation
52:formed by three, usually
317:10.1073/pnas.1011218107
344:-related article is a
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195:Godbey, W.T. (2014),
70:quaternary structure.
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54:non-covalently bound
176:Trimer (chemistry)
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400:Protein complexes
395:Protein structure
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103:heterotrimer
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82:polypeptides
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39:biochemistry
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78:hydrophilic
74:hydrophobic
389:Categories
266:2024-05-03
224:2024-05-03
197:"Proteins"
182:References
94:homotrimer
99:molecules
292:14149958
166:Oligomer
160:See also
107:Collagen
86:oligomer
62:proteins
342:protein
132:alleles
50:complex
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129:mutant
113:Porins
340:This
60:like
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346:stub
288:PMID
255:ISBN
213:ISBN
125:gene
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