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Thermal behavior of proteins: Heat-resistant proteins and their heat-induced secondary structural changes

Authors
 Thomas D. Kim  ;  Hyun Jeong Ryu  ;  Hyun Il Cho  ;  Chul-Hak Yang  ;  Jongsun Kim 
Citation
 Biochemistry, Vol.39(48) : 14839-14846, 2000 
Journal Title
 Biochemistry 
ISSN
 0006-2960 
Issue Date
2000
MeSH
Amino Acid Sequence ; Apolipoprotein A-I/chemistry ; Blood Proteins/chemistry* ; Caseins/chemistry ; Circular Dichroism ; Hot Temperature* ; Humans ; Jurkat Cells ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry ; Prealbumin/chemistry ; Protein Denaturation* ; Protein Folding ; Protein Structure, Secondary* ; Sequence Analysis, Protein ; Synucleins ; alpha-Fetoproteins/chemistry ; alpha-Synuclein
Abstract
Most proteins are denatured by heat treatment, and the process is usually irreversible. However, some proteins, such as hyperthermophilic proteins are known to be stable even at the boiling temperature of water. We here describe a systematic investigation of thermal behavior of proteins by purifying and characterizing some heat-resistant proteins (HRPs) that are not aggregated upon heat treatment. Although most proteins were precipitated by boiling in a water bath, about 20 and 70 wt % of total proteins appeared to be heat-resistant in Jurkat T-cell lysates and human serum, respectively. We identified major HRPs from Jurkat T-cells and human serum by N-terminal amino acid sequencing and Western blot analysis. HRPs of 20 and 45 kDa (HRP20 and HRP45) were identified as alpha-synuclein and calreticulin, respectively, and HRPs of 60, 27, and 16 kDa (HRP60, HRP27, and HRP16) were identified as human serum fetuin, apolipoprotein A-I, and transthyretin, respectively. By a systematic investigation of the effect of heat on the secondary structure of the purified HRPs by circular dichroic spectroscopy, we observed four major types of thermal behavior, suggesting that the proteins could protect themselves through these pathways. Although our analysis is restricted to protein secondary structural changes, our data indicate that heat resistance of protein can be achieved in several different ways depending on the thermodynamic stability of native (N), unfolded (U), denatured (D), and intermediate (I) states.
Full Text
https://pubs.acs.org/doi/abs/10.1021/bi001441y
DOI
10.1021/bi001441y
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/171569
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