Tags

Type your tag names separated by a space and hit enter

Deciphering the molecular structure of cryptolepain in organic solvents.
Biochimie. 2012 Feb; 94(2):310-7.B

Abstract

Solvent composition plays a major role in stabilizing/destabilizing the forces that are responsible for the native structure of a protein. Often, the solvent composition drives the protein into non-native conformations. Elucidation of such non-native structures provides valuable information about the molecular structure of the protein, which is unavailable otherwise. Inclusion of methanol (non-fluorinated alcohol) or TFE (fluorinated alcohol) in the solvent composition drove cryptolepain, a serine protease and an all-β-protein, into a non-native structure with an enhanced β-sheet or induction of α-helix. These solvents did not much affect cryptolepain under neutral conditions, even at higher concentrations, but the effects were predominant at lower pH, when the protein molecule is under stress. The organic solvent-induced state is partially unfolded with similar characteristics to the molten globule state seen with protein under a variety of conditions. Chemical- or temperature-induced unfolding of cryptolepain in the presence of organic solvent is distinctly different from that in the absence of organic solvent. Such different unfolding provided evidence of two structural variants in the molecular structure of the protein as well as the differential stabilization/destabilization of such structural variants and their sequential unfolding.

Authors+Show Affiliations

Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, Varanasi 221005, India.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21820031

Citation

Prasanna Kumari, N K., and M V. Jagannadham. "Deciphering the Molecular Structure of Cryptolepain in Organic Solvents." Biochimie, vol. 94, no. 2, 2012, pp. 310-7.
Prasanna Kumari NK, Jagannadham MV. Deciphering the molecular structure of cryptolepain in organic solvents. Biochimie. 2012;94(2):310-7.
Prasanna Kumari, N. K., & Jagannadham, M. V. (2012). Deciphering the molecular structure of cryptolepain in organic solvents. Biochimie, 94(2), 310-7. https://doi.org/10.1016/j.biochi.2011.07.017
Prasanna Kumari NK, Jagannadham MV. Deciphering the Molecular Structure of Cryptolepain in Organic Solvents. Biochimie. 2012;94(2):310-7. PubMed PMID: 21820031.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Deciphering the molecular structure of cryptolepain in organic solvents. AU - Prasanna Kumari,N K, AU - Jagannadham,M V, Y1 - 2011/07/27/ PY - 2011/01/04/received PY - 2011/07/13/accepted PY - 2011/8/9/entrez PY - 2011/8/9/pubmed PY - 2012/6/12/medline SP - 310 EP - 7 JF - Biochimie JO - Biochimie VL - 94 IS - 2 N2 - Solvent composition plays a major role in stabilizing/destabilizing the forces that are responsible for the native structure of a protein. Often, the solvent composition drives the protein into non-native conformations. Elucidation of such non-native structures provides valuable information about the molecular structure of the protein, which is unavailable otherwise. Inclusion of methanol (non-fluorinated alcohol) or TFE (fluorinated alcohol) in the solvent composition drove cryptolepain, a serine protease and an all-β-protein, into a non-native structure with an enhanced β-sheet or induction of α-helix. These solvents did not much affect cryptolepain under neutral conditions, even at higher concentrations, but the effects were predominant at lower pH, when the protein molecule is under stress. The organic solvent-induced state is partially unfolded with similar characteristics to the molten globule state seen with protein under a variety of conditions. Chemical- or temperature-induced unfolding of cryptolepain in the presence of organic solvent is distinctly different from that in the absence of organic solvent. Such different unfolding provided evidence of two structural variants in the molecular structure of the protein as well as the differential stabilization/destabilization of such structural variants and their sequential unfolding. SN - 1638-6183 UR - https://www.unboundmedicine.com/medline/citation/21820031/Deciphering_the_molecular_structure_of_cryptolepain_in_organic_solvents_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0300-9084(11)00275-6 DB - PRIME DP - Unbound Medicine ER -