Thermal stability of calf skin collagen type I in salt solutions.


Abstract

The thermal stability of acid-soluble collagen type I from calf skin in salt solutions is studied by high-sensitivity differential scanning calorimetry. Three concentration ranges have been clearly distinguished in the dependence of collagen thermal stability on ion concentration. At concentrations below 20 mM, all studied salts reduce the temperature of collagen denaturation with a factor of about 0.2 degree C per 1 mM. This effect is attributed to screening of electrostatic interactions leading to collagen stabilisation. At higher concentrations, roughly in the range 20-500 mM, the different salts either slightly stabilise or further destabilise the collagen molecule in salt-specific way that correlates with their position in the lyotropic series. The effect of anions is dominating and follows the order H2PO4- > or = SO4(2-) > Cl- > SCN-, with sign inversion at about SO4(2-). This effect, generally known as the Hofmeister effect, is associated with indirect protein-salt interactions exerted via competition for water molecules between ions and the protein surface. At still higher salt concentrations (onset concentrations between 200 and 800 mM for the different salts), the temperature of collagen denaturation and solution opacity markedly increase for all studied salts due to protein salting out and aggregation. The ability of salts to salt out collagen also correlates with their position in the lyotropic series and increases for chaotropic ions. The SO4(2-) anions interact specifically with collagen - they induce splitting of the protein denaturation peak into two components in the range 100-150 mM Na2SO4 and 300-750 mM Li2SO4. The variations of the collagen denaturation enthalpy at low and intermediate salt concentrations are consistent with a weak linear increase of the enthalpy with denaturation temperature. Its derivative, d(delta H)/dT, is approximately equal to the independently measured difference in the heat capacities of the denatured and native states, delta Cp = Cp(D) - Cp(N) approximately 0.1 cal.g-1 K-1. Study holds ProTherm entries: 9371 Extra Details: collagen type I; protein-salt interactions; thermal stability DSC; protein electrostatics; Hofmeister effect; (calf skin)

Submission Details

ID: bzjDjL5P

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:37 p.m.

Version: 1

Publication Details
Komsa-Penkova R;Koynova R;Kostov G;Tenchov BG,Biochim. Biophys. Acta (1996) Thermal stability of calf skin collagen type I in salt solutions. PMID:8917619
Additional Information

Study Summary

Number of data points 1
Proteins Collagen alpha-1(I) chain
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: Tm
Libraries Mutations for sequence MFSFVDLRLLLLLAATALLTHGQEEGQEEGQEEDIPPVTCVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELKDCPNAKVPTDECCPVCPEGQESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEGGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGPPGPKGNSGEPGAPGSKGDTGAKGEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLTGPIGPPGPAGAPGDKGEAGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDAGPAGPPGPPGPPGPPGPPSGGYDLSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKEKRHVWYGESMTGGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACFL

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2LLP 2012-05-30 Solution structure of a THP type 1 alpha 1 collagen fragment (772-786)
5CTD 2016-08-03 1.6 Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 of type I collagen
1Q7D 2004-01-13 1.8 Structure of the integrin alpha2beta1 binding collagen peptide
5CTI 2016-08-03 1.9 Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 of type I collagen (native form)
5CVA 2016-08-10 2.1 Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen
3EJH 2009-02-03 2.1 Crystal Structure of the Fibronectin 8-9FnI Domain Pair in Complex with a Type-I Collagen Peptide
5K31 2017-03-22 2.2 Crystal structure of Human fibrillar procollagen type I C-propeptide Homo-trimer
5CVB 2016-08-10 2.25 Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a1a1 of type I collagen
5OU8 2018-09-05 2.5 Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)5
5OU9 2018-09-05 2.5 Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)3
3GXE 2010-04-07 2.6 Complex of a Low Affinity Collagen Site with the Fibronectin 8-9FnI Domain Pair
3HR2 2009-07-14 5.16 Low resolution, molecular envelope structure of type I collagen in situ determined by fiber diffraction. Single type I collagen molecule, post rigid body refinement, 'relaxed'
3HQV 2009-07-14 5.16 Low resolution, molecular envelope structure of type I collagen in situ determined by fiber diffraction. Single type I collagen molecule, rigid body refinement

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
91.1 Collagen alpha-1(I) chain P11087 CO1A1_MOUSE
91.1 Collagen alpha-1(I) chain P02454 CO1A1_RAT
97.4 Collagen alpha-1(I) chain P02452 CO1A1_HUMAN
97.4 Collagen alpha-1(I) chain Q9XSJ7 CO1A1_CANLF
100.0 Collagen alpha-1(I) chain P02453 CO1A1_BOVIN