Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1996-12-24
pubmed:abstractText
Isothermal titration microcalorimetry is combined with solution-depletion isotherm data to analyze the thermodynamics of binding of the cellulose-binding domain (CBD) from the beta-1,4-(exo)glucanase Cex of Cellulomonas fimi to insoluble bacterial microcrystalline cellulose. Analysis of isothermal titration microcalorimetry data against two putative binding models indicates that the bacterial microcrystalline cellulose surface presents two independent classes of binding sites, with the predominant high-affinity site being characterized by a Langmuir-type Ka of 6.3 (+/-1.4) x 10(7) M-1 and the low-affinity site by a Ka of 1.1 (+/-0.6) x 10(6) M-1. CBDCex binding to either site is exothermic, but is mainly driven by a large positive change in entropy. This differs from protein binding to soluble carbohydrates, which is usually driven by a relatively large exothermic standard enthalpy change for binding. Differential heat capacity changes are large and negative, indicating that sorbent and protein dehydration effects make a dominant contribution to the driving force for binding.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-1367528, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-1409557, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-1551882, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-1619648, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-1886523, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-2207096, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-2481445, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-2494059, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-2757186, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-2791755, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-3134347, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-3800965, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-4602947, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-5166895, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-5391868, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-7513555, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-7766609, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-7925430, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-8196546, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-8246788, http://linkedlifedata.com/resource/pubmed/commentcorrection/8901562-8540419
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12229-34
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Binding of the cellulose-binding domain of exoglucanase Cex from Cellulomonas fimi to insoluble microcrystalline cellulose is entropically driven.
pubmed:affiliation
Department of Chemical Engineering, University of British Columbia, Vancouver, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't