Publication Date:
1992-09-11
Description:
A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution. Nuclear Overhauser effect (NOE) measurements with a 7 molar urea solution of the amino-terminal 63-residue domain of the 434-repressor and distance geometry calculations showed that the polypeptide segment 54 to 59 forms a hydrophobic cluster containing the side chains of Val54, Val56, Trp58, and Leu59. This residual structure in the urea-unfolded protein is related to the corresponding region of the native, folded protein by simple rearrangements of the residues 58 to 60. Based on these observations a model for the early phase of refolding of the 434-repressor(1-63) is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neri, D -- Billeter, M -- Wider, G -- Wuthrich, K -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1559-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Biophysik, ETH-Honggerberg, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1523410" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Magnetic Resonance Spectroscopy/methods
;
Models, Molecular
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Denaturation
;
Repressor Proteins/*chemistry/pharmacology
;
Urea/*pharmacology
;
Viral Proteins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink