Asher SA - Search Results

1

UV resonance Raman study of angiotensin II conformation in nonaqueous environments: lipid micelles and acetonitrile.

Holtz JS, Lednev IK, Asher SA. Holtz JS, et al. Among authors: asher sa. Biopolymers. 2000;57(2):55-63. doi: 10.1002/(SICI)1097-0282(2000)57:2<55::AID-BIP2>3.0.CO;2-B. Biopolymers. 2000. PMID: 10766956

2

Ultraviolet resonance Raman and absorption difference spectroscopy of myoglobins: titration behavior of individual tyrosine residues.

Asher SA, Larkin PJ, Teraoka J. Asher SA, et al. Biochemistry. 1991 Jun 18;30(24):5944-54. doi: 10.1021/bi00238a019. Biochemistry. 1991. PMID: 2043634

3

UV resonance Raman studies of molecular structure and dynamics: applications in physical and biophysical chemistry.

Asher SA. Asher SA. Annu Rev Phys Chem. 1988;39:537-88. doi: 10.1146/annurev.pc.39.100188.002541. Annu Rev Phys Chem. 1988. PMID: 3075468 Review. No abstract available.

4

UV resonance Raman and excited-state relaxation rate studies of hemoglobin.

Cho N, Song S, Asher SA. Cho N, et al. Among authors: asher sa. Biochemistry. 1994 May 17;33(19):5932-41. doi: 10.1021/bi00185a034. Biochemistry. 1994. PMID: 8180222

5

UV resonance Raman-selective amide vibrational enhancement: quantitative methodology for determining protein secondary structure.

Chi Z, Chen XG, Holtz JS, Asher SA. Chi Z, et al. Among authors: asher sa. Biochemistry. 1998 Mar 3;37(9):2854-64. doi: 10.1021/bi971160z. Biochemistry. 1998. PMID: 9485436

6

UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse myoglobin.

Chi Z, Asher SA. Chi Z, et al. Among authors: asher sa. Biochemistry. 1998 Mar 3;37(9):2865-72. doi: 10.1021/bi971161r. Biochemistry. 1998. PMID: 9485437

7

Ultraviolet Raman examination of the environmental dependence of bombolitin I and bombolitin III secondary structure.

Holtz JS, Holtz JH, Chi Z, Asher SA. Holtz JS, et al. Among authors: asher sa. Biophys J. 1999 Jun;76(6):3227-34. doi: 10.1016/S0006-3495(99)77474-6. Biophys J. 1999. PMID: 10354447 Free PMC article.

8

Ultraviolet resonance Raman examination of horse apomyoglobin acid unfolding intermediates.

Chi Z, Asher SA. Chi Z, et al. Among authors: asher sa. Biochemistry. 1999 Jun 29;38(26):8196-203. doi: 10.1021/bi982654e. Biochemistry. 1999. PMID: 10387065

9

Transient UV Raman spectroscopy finds no crossing barrier between the peptide alpha-helix and fully random coil conformation.

Lednev IK, Karnoup AS, Sparrow MC, Asher SA. Lednev IK, et al. Among authors: asher sa. J Am Chem Soc. 2001 Mar 14;123(10):2388-92. doi: 10.1021/ja003381p. J Am Chem Soc. 2001. PMID: 11456888

10

UV Raman studies of peptide conformation demonstrate that betanova does not cooperatively unfold.

Boyden MN, Asher SA. Boyden MN, et al. Among authors: asher sa. Biochemistry. 2001 Nov 13;40(45):13723-7. doi: 10.1021/bi011505k. Biochemistry. 2001. PMID: 11695921

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