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17 de abril de 2014

Site Departamentos  »  Química Orgânica  »  Docentes



Carlos Henrique Inacio Ramos



Formação Acadêmica


MS-5; Professor Associado; Bel. Biol-Bioq. (UFMG-1991); Dr. Bioquímica (USP-1996); Pós-doutorado (Stanford Univ. EUA - 12/1996 - 12/1998); Livre -docente Bioquímica (USP-2005).

Contato


Sala E-203
Fax: +55-19-3521-3023
Fone: +55-19-3521-3096 (sala)
Fone: +55-19-3521-3020 (laboratório)
Currículo Lattes
cramos@iqm.unicamp.br

Pesquisa


Bioquímica de proteínas:

.enovelamento e estabilidade de globinas

.estrutura e função de chaperonas moleculares

.enovelamento incorreto e doenças conformacionais

.caracterização físico-química de proteínas

Publicação


1. Ramos,C.H.I., Weisbuch,S., Jamin,M. (2007) Diffusive motions control the folding and unfolding kinetics of apomyoglobin pH 4 molten globule intermediate. Biochemistry 46, 4379-4389.

2. Tiroli, A.O., Ramos, C.H.I. (2007). Biochemical and biophysical characterization of small heat shock proteins from sugarcane. Involvement of a specific region located at the N-terminus with substrate specificity. International Journal of Biochemistry and Cell Biology 39, 818-831.

3. Borges, J.C., Ramos, C.H.I. (2006). Spectroscopic and thermodynamic measurements of nucleotide-induced changes in the human 70-kDa heat shock cognate protein. Archives of Biochemistry and Biophysics 452, 46-54.

4. Ribeiro-Jr, E.A., Ramos, C.H.I. (2005). Circular permutation and deletion studies of myoglobin indicate that the correct position of its N-terminus is required for native stability and solubility but not for native-like heme binding and folding. Biochemistry 44, 4699-4709.

5. Borges, J.C., Hannes, F., Craievich, A.F., Ramos, C.H.I. (2005). Low-resolution structural study of two human Hsp40 chaperones in solution. HJA1 from subfamily A and HJB4 from subfamily B, have different quaternary structures. Journal of Biological Chemistry 280, 13671-13681.

6. Ramos, C.H.I., Ferreira, S.T. (2005). Protein folding, misfolding and aggregation: evolving concepts and conformational diseases. Protein & Peptide Letters 12, 213-222.









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