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Items: 9

2.

Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin.

Murray LP, Hofrichter J, Henry ER, Eaton WA.

Biophys Chem. 1988 Feb;29(1-2):63-76. Review.

PMID:
3282562
3.

Utility of heme analogues to intentionally modify heme-globin interactions in myoglobin.

Neya S, Nagai M, Nagatomo S, Hoshino T, Yoneda T, Kawaguchi AT.

Biochim Biophys Acta. 2016 May;1857(5):582-8. doi: 10.1016/j.bbabio.2015.09.009. Epub 2015 Oct 3. Review.

4.

Fast natural and magnetic circular dichroism spectroscopy.

Goldbeck RA, Kim-Shapiro DB, Kliger DS.

Annu Rev Phys Chem. 1997;48:453-79. Review.

PMID:
9348661
5.

Probing kinetic mechanisms of protein function and folding with time-resolved natural and magnetic chiroptical spectroscopies.

Kliger DS, Chen E, Goldbeck RA.

Int J Mol Sci. 2012;13(1):683-97. doi: 10.3390/ijms13010683. Epub 2012 Jan 10. Review.

6.

Picosecond infrared spectroscopy of hemoglobin and myoglobin.

Austin RH, Rothberg LJ.

Methods Enzymol. 1994;232:176-204. Review. No abstract available.

PMID:
8057860
7.

Real-time spectroscopic techniques for probing conformational dynamics of heme proteins.

Dunn RC, Xie X, Simon JD.

Methods Enzymol. 1993;226:177-98. Review. No abstract available.

PMID:
8277865
8.

Nanosecond time-resolved absorption and polarization dichroism spectroscopies.

Goldbeck RA, Kliger DS.

Methods Enzymol. 1993;226:147-77. Review. No abstract available.

PMID:
8277864
9.

Stationary and time-resolved circular dichroism of hemoglobins.

Zentz C, Pin S, Alpert B.

Methods Enzymol. 1994;232:247-66. Review. No abstract available.

PMID:
8057863

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