Document Detail


Exploring unique structures: flexibility is a significant factor in biological activity.
MedLine Citation:
PMID:  17541149     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The effect of molecular flexibility on biological activity was described for soft (e.g. hGH peptides) and hard molecules (e.g. biscoclaurine-type alkaloids). These molecules had a macrocyclic structure during molecular mechanics analysis, and the minimum essential unit, which affects insulin-involved fatty acid synthesis, was observed. The flexibility of the molecular center is concerning with biological activity through the diversification of structural feature, and compared with two types of molecules which have a rigid (haloacetylcarbamoyl-2-nitroimidazole analogs: chiral-TXs) or flexible (bis-quaternary ammonium compounds: bis-QACs) molecular center. Center flexibility reflected the conformation occurrence in TXs and bis-QACs. A parameter (solvation-free energy: dGW), which reflects structural hydrophobicity, was shown, and applied to the molecular design of brefeldin A analog. This hydrophobic index was very useful, and was used for conformational analysis of chiral-TXs and bis-QACs. In molecular dynamics analysis of cholesterol-dependent cytolysin (e.g. streptolysin O) and -independent cytolysin (e.g. intermedilysin), whole molecules moved like a bow and different conformations were shown in every moment. In such situations, the membrane-associated 11mer region in these cytolysins were flexible and could always interact with extramolecular factors (e.g. membrane constitution).
Authors:
Kazuto Ohkura
Related Documents :
21827939 - Nipped in the bud: how the amsh mit domain helps deubiquitinate lysosome-bound cargo.
11933259 - Preorganization and protein dynamics in enzyme catalysis.
17822439 - Structural flexibility in trypanosoma brucei enolase revealed by x-ray crystallography ...
21651889 - Influence of detergents on the activity of the abc transporter lmra.
8820489 - Fitting an inhibitor into the active site of thermolysin: a molecular dynamics case study.
15780269 - Potential transition-state analogs for glycosyltransferases. design and dft calculation...
22406519 - A fungal ketoreductase domain that displays substrate-dependent stereospecificity.
8140099 - A pore-forming protein with a protease-activated trigger.
25372689 - Structure-specificity relationships in abp, a gh27 β-l-arabinopyranosidase from geobaci...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Biological & pharmaceutical bulletin     Volume:  30     ISSN:  0918-6158     ISO Abbreviation:  Biol. Pharm. Bull.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-01     Completed Date:  2007-07-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9311984     Medline TA:  Biol Pharm Bull     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1025-36     Citation Subset:  IM    
Affiliation:
Faculty of Pharmacy, Chiba Institute of Science, Japan. kohkura@sag.bekkoame.ne.jp
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Computer Simulation
Humans
Hydrophobicity
Molecular Conformation
Molecular Structure
Peptides / chemistry
Protein Binding
Protein Conformation*
Protein Structure, Secondary
Protein Structure, Tertiary
Stereoisomerism
Structure-Activity Relationship
Thermodynamics
Chemical
Reg. No./Substance:
0/Peptides

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Spontaneous intracranial hypotension--a case report and discussion
Next Document:  Anti-inflammatory effect of oyaksungisan in peripheral blood mononuclear cells from cerebral infarct...