Allotment of carbon is responsible for disorders in proteins

Ekambaram, Rajasekaran; Akila, K.; Vijayasarathy, Marimuthu

doi:10.6026/97320630006291

Cited by 10 publications

(13 citation statements)

References 5 publications

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“…Allotment of carbon is responsible for disorders in proteins [4]. The carbon distribution analysis in disordered proteins is the focus of this work by taking neurodegenerative protein.…”

Section: Introductionmentioning

confidence: 99%

Study on Carbon Distribution at Protein Regions of Disorder

Akila¹,

Sneha²,

Ekambaram³

2012

IJBBB

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Abstract-Hydrophobic interaction is the dominant force in proteins that arises due to carbon. The content and distribution of this carbon make a protein to fold in some form to have a specific function. Diseased proteins are expectedly differing from this carbon distribution pattern. This is taken as focus of this work by taking neurodegenerative protein, the SOD for study. The carbon distribution analysis program is able to identify the disordered region clearly. A long stretch of hydrophilic/hydrophobic regions with different combination of amino acid is considered as disordered regions. This disorder is due to unfolding or misfolding. The program developd for this purpose can further analysis the proteins for identification of mutational sites for stabilisation.

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“…Allotment of carbon is responsible for disorders in proteins [4]. The carbon distribution analysis in disordered proteins is the focus of this work by taking neurodegenerative protein.…”

Section: Introductionmentioning

confidence: 99%

Study on Carbon Distribution at Protein Regions of Disorder

Akila¹,

Sneha²,

Ekambaram³

2012

IJBBB

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“…These mutants at residue position 30, 33 and 36 were characterized by broadened distribution curve for carbon content with decreased carbon frequency peak thus destabilized protein function in terms of its sweetness. Broadened carbon distribution curve with decreased frequency peak destabilizes the structure and possibly leading to loss of protein functionality [12,14]. Based on carbon distribution analysis on several numbers of proteins, it has previously been reported that at mutation site, a single mutation can alter the protein function [17,18].…”

Section: Discussionmentioning

confidence: 99%

“…The residues specifically examined were in position number 29, 30, 31, 33, 36, 41 and 43. In order to elucidate the variation between mutants with increased brazzein sweetness and the mutants with decreased brazzein sweetness, analysis for local carbon density at the mutational sites was done along brazzein protein sequences for the mutants using a protein sequence CARD program for carbon [12,13].The carbon content distribution profile outputs of Carbana and sequence CARD were then plotted for better visualization of results. For the analysis of the carbon distribution profile for brazzein sequences both the wild-type and mutants, the Carbana software available online (www.rajasekaran.net.in/tools/carbana.html) was used.…”

Section: Methodsmentioning

confidence: 99%

“…The role of carbon content and its distribution along in protein sequences has rarely been investigated in relation to mutation in proteins although carbon is the main architectural component of proteins. Amino acids can vary significantly in their contents of specific individual atoms such as carbon which has a potential of revealing hydrophobic and hydrophilic regions in the protein [12][13][14]. The purpose of the current study was to investigate how the carbon content distribution is useful in examining brazzein protein stability and its function upon mutations.…”

Section: Introductionmentioning

confidence: 99%

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The Effect of Mutation in Brazzein Deduced from Mutational Sites and Sequence Carbon Content

Amri¹

2015

IJGG

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Abstract:Brazzein is a small sweet-tasting protein isolated from the fruit of the African plant, Pentadiplandra brazzeana Baillon with potential of replacement of carbohydrate sweeteners. Carbon content analysis was used to examine the effect of mutation in brazzein's two regions at residues 29-33 and 39-43 with residue 36 reported to be important in sweet tasting of the protein. Analysis for local carbon density at the mutational sites for brazzein mutants with increased sweetness taste at residues 29 and 41 revealed normal carbon distribution curves with increased carbon frequency peak compared to the wild-type, consequently stabilized the local structure. Brazzein mutants with reduced sweetness taste at residue position 30, 33, 36 and 43 were mostly characterized by abnormal broadened distribution curve for carbon content with decreased frequency peak which destabilized the local structure and possibly leading to loss of protein functionality. Further analysis of carbon distribution profile along protein sequences of brazzein revealed a variation in carbon distribution between mutants with increased sweetness taste and those with decreased sweetness taste. Mutants with increased sweetness taste had carbon distribution profile balancing well conforming to the globular proteins which prefers to have 31.45% of carbon all along the sequence for stability. This study has provided further information and additional insights into protein atomic composition in brazzein and its role in understanding the effect of mutation.

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“…When there is inadequate carbon point of distribution where alteration can be performed by probe binding at the adjacent site effectively. Accordingly initiatives are done to probe the role of carbon in dealing with other situations like, pattern recognition, 7,8 disorders in protein, 9,10 disease causing 11,12 and mutational role [11][12][13][14][15] when other forces fail to capture the essence of it. When in need one can probe those devisable mechanisms for possible arrangements to continue with carbon value based method of alternative design and action actually taken here.…”

Section: Introductionmentioning

confidence: 99%

Domain formation in regions of protein probe interaction

Ekambaram¹,

Rajasekaran²,

Meenal³

2019

IJMBOA

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One of the interesting focus points of research in protein science is the active site analysis and probe fixing. Overall one can go on searching this interesting phenomenon of probe fixing but without proper explanation on how and why this happens at some site neglecting other places. One of the probe fixing methods could be come along the way of newly discovered carbon role in protein stability that is taken here as starting point for due course of action. Carbon role in protein domain formation and active portion are interestingly yielded good result. Analysis includes ICOD of protein in native and domain state of active portion in complex protein. ICOD analysis reveals that carbon does play an interesting role in probe of action. Alternative method to detect active portion and probe development can be better exploited from this carbon domain of protein for life science to excel.

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Allotment of carbon is responsible for disorders in proteins

Cited by 10 publications

References 5 publications

Study on Carbon Distribution at Protein Regions of Disorder

Study on Carbon Distribution at Protein Regions of Disorder

The Effect of Mutation in Brazzein Deduced from Mutational Sites and Sequence Carbon Content

Domain formation in regions of protein probe interaction

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